+publisher:"University of Texas – Austin" +contributor:("Macdonald, Paul")

University of Texas – Austin

1. Gim, Youme. Bruno contributes to osk mRNA localization during Drosophila oogenesis: Bruno contributes to oskar messenger RNA localization during Drosophila oogenesis.

Degree: MA, Cell and Molecular Biology, 2011, University of Texas – Austin

URL: http://hdl.handle.net/2152/41734

► Oskar is a body pattern and germ cell determining protein in Drosophila melanogaster. This protein must be properly expressed to ensure correct formation of the… (more)

Subjects/Keywords: Oskar; Bruno; mRNA localization

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Gim, Y. (2011). Bruno contributes to osk mRNA localization during Drosophila oogenesis: Bruno contributes to oskar messenger RNA localization during Drosophila oogenesis. (Masters Thesis). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/41734

Chicago Manual of Style (16^th Edition):

Gim, Youme. “Bruno contributes to osk mRNA localization during Drosophila oogenesis: Bruno contributes to oskar messenger RNA localization during Drosophila oogenesis.” 2011. Masters Thesis, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/41734.

MLA Handbook (7^th Edition):

Gim, Youme. “Bruno contributes to osk mRNA localization during Drosophila oogenesis: Bruno contributes to oskar messenger RNA localization during Drosophila oogenesis.” 2011. Web. 27 Feb 2021.

Vancouver:

Gim Y. Bruno contributes to osk mRNA localization during Drosophila oogenesis: Bruno contributes to oskar messenger RNA localization during Drosophila oogenesis. [Internet] [Masters thesis]. University of Texas – Austin; 2011. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/41734.

Council of Science Editors:

Gim Y. Bruno contributes to osk mRNA localization during Drosophila oogenesis: Bruno contributes to oskar messenger RNA localization during Drosophila oogenesis. [Masters Thesis]. University of Texas – Austin; 2011. Available from: http://hdl.handle.net/2152/41734

University of Texas – Austin

2. Ryu, Young Hee. The role of Bicoid Stability Factor in oskar mRNA function and regulation, and the mechanisms for oskar mRNA transport to the oocyte.

Degree: PhD, Cell and Molecular Biology, 2015, University of Texas – Austin

URL: http://hdl.handle.net/2152/46755

► My dissertation is separated into two subjects. First, I examined the role of Bicoid Stability Factor (BSF) in oskar (osk) regulation. Second, I studied cis-acting… (more)

▼ My dissertation is separated into two subjects. First, I examined the role of Bicoid Stability Factor (BSF) in oskar (osk) regulation. Second, I studied cis-acting elements involved in osk mRNA transport to the oocyte during early oogenesis. Oskar (Osk) is a body patterning determinant in Drosophila and is highly concentrated at the posterior pole of the oocyte. This spatially-restricted deployment relies on a coordinated program of osk mRNA localization and translational regulation, all dependent on cis-acting regulatory elements located primarily in the 3’ UTR of the mRNA. Notably, some of these elements, as well as sequences required for a noncoding role of osk mRNA, are clustered in a short region (the C region) near the 3’ end of the osk mRNA. To better understand the role of the C region, I searched for proteins that bind specifically to this region and I found BSF. Binding assays to mutant RNAs suggested that BSF does not act in the noncoding function of osk mRNA. To test for a role for BSF in regulation of Osk protein expression, I used two complementary approaches, reducing the BSF level or disrupting BSF binding to the osk mRNA. Both generated similar results: a reduction or loss of posterior Osk protein and osk mRNA in late oogenesis and early embryogenesis, while the level of osk mRNA was not affected. My work suggests that BSF could act in a late phase of osk mRNA localization or translational activation. Localization of osk mRNA to the posterior pole of the oocyte is achieved by multiple transport steps. One is mRNA transport from the nurse cells to the oocyte. Although cis-acting elements including the oocyte entry signal (OES) in the osk mRNA 3’ UTR have been implicated in mRNA oocyte transport, the precise mechanisms remain unknown. Here, I show that the clusters of Bru binding sites in the osk mRNA 3’ UTR required for translational regulation confer oocyte transport on a reporter mRNA. However, neither Bru sites nor the OES are essential for oocyte transport of osk mRNA. This suggests that there are multiple mechanisms redundantly acting in oocyte transport. Advisors/Committee Members: Macdonald, Paul M. (advisor), Fischer, Janice (committee member), Stein, David (committee member), Sullivan, Christopher (committee member), Vokes, Steven (committee member).

Subjects/Keywords: Oskar; Osk; BSF; mRNA localization; Translational activation; Bicoid Stability Factor; Oocytes; Oogenesis; Drosophila; Cis-acting elements

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Ryu, Y. H. (2015). The role of Bicoid Stability Factor in oskar mRNA function and regulation, and the mechanisms for oskar mRNA transport to the oocyte. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/46755

Chicago Manual of Style (16^th Edition):

Ryu, Young Hee. “The role of Bicoid Stability Factor in oskar mRNA function and regulation, and the mechanisms for oskar mRNA transport to the oocyte.” 2015. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/46755.

MLA Handbook (7^th Edition):

Ryu, Young Hee. “The role of Bicoid Stability Factor in oskar mRNA function and regulation, and the mechanisms for oskar mRNA transport to the oocyte.” 2015. Web. 27 Feb 2021.

Vancouver:

Ryu YH. The role of Bicoid Stability Factor in oskar mRNA function and regulation, and the mechanisms for oskar mRNA transport to the oocyte. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2015. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/46755.

Council of Science Editors:

Ryu YH. The role of Bicoid Stability Factor in oskar mRNA function and regulation, and the mechanisms for oskar mRNA transport to the oocyte. [Doctoral Dissertation]. University of Texas – Austin; 2015. Available from: http://hdl.handle.net/2152/46755

University of Texas – Austin

3. -1021-0306. Mechanisms directing chondrocyte specification in the developing limb.

Degree: PhD, Cell and Molecular Biology, 2018, University of Texas – Austin

URL: http://hdl.handle.net/2152/68374

► During limb development, skeletal elements originate from highly proliferative mesodermal progenitor cells that differentiate into chondrocytes. While this process must be tightly regulated to ensure… (more)

Subjects/Keywords: BMP; Prmt5; Limb development; Polydactyly; Chondrogenesis; Chondroprogenitor; Gremlin; Sox9

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

-1021-0306. (2018). Mechanisms directing chondrocyte specification in the developing limb. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/68374

Note: this citation may be lacking information needed for this citation format:
Author name may be incomplete

Chicago Manual of Style (16^th Edition):

-1021-0306. “Mechanisms directing chondrocyte specification in the developing limb.” 2018. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/68374.

Note: this citation may be lacking information needed for this citation format:
Author name may be incomplete

MLA Handbook (7^th Edition):

-1021-0306. “Mechanisms directing chondrocyte specification in the developing limb.” 2018. Web. 27 Feb 2021.

Note: this citation may be lacking information needed for this citation format:
Author name may be incomplete

Vancouver:

-1021-0306. Mechanisms directing chondrocyte specification in the developing limb. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2018. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/68374.

Note: this citation may be lacking information needed for this citation format:
Author name may be incomplete

Council of Science Editors:

-1021-0306. Mechanisms directing chondrocyte specification in the developing limb. [Doctoral Dissertation]. University of Texas – Austin; 2018. Available from: http://hdl.handle.net/2152/68374

Note: this citation may be lacking information needed for this citation format:
Author name may be incomplete

University of Texas – Austin

4. Wolfe, Sarah Anne. Molecular mechanisms underlying alcohol use disorder and major depressive disorder comorbidity.

Degree: PhD, Cellular and Molecular Biology, 2017, University of Texas – Austin

URL: http://dx.doi.org/10.26153/tsw/2231

► Alcohol Use Disorder (AUD) and Major Depressive Disorder (MDD) are two widespread and debilitating disorders that share a high rate of comorbidity with the presence… (more)

▼ Alcohol Use Disorder (AUD) and Major Depressive Disorder (MDD) are two widespread and debilitating disorders that share a high rate of comorbidity with the presence of either disorder doubling the risk of developing the other. Despite their prevalence, few treatments are available to individuals with comorbid AUD and MDD. Both alcohol and antidepressants promote lasting neuroadaptive changes in synapses and dendrites. With alcohol these changes may provide relief from depressive symptoms, and the initial use of alcohol may be a form of self-medication for individuals with MDD, suggesting ethanol may have antidepressant properties underlying similarities in neurobiological abnormalities. However, the synaptic pathways that are shared by alcohol and antidepressants are unknown. This study aims to identify why acute exposure to ethanol produced lasting antidepressant and anxiolytic behaviors. To understand the functional basis of these behaviors, a molecular pathway activated by rapid antidepressants was investigated. Here ethanol, like rapid antidepressants, altered γ-aminobutyric acid type B receptor (GABA [subscript B] R) expression and signaling, to increase dendritic calcium. New GABA [subscript B] Rs were synthesized in response to ethanol treatment, requiring fragile-X mental retardation protein (FMRP). Ethanol-dependent changes in GABA [subscript B] R expression, dendritic signaling, and antidepressant efficacy were absent in Fmr1-knockout (KO) mice. These findings indicate that FMRP is an important regulator of protein synthesis following acute alcohol exposure, and provided a molecular basis for the antidepressant efficacy of acute ethanol exposure. We identify alterations on a global scale with acute alcohol and antidepressant by sequencing the synaptic transcriptome. We identified parallel alterations in exon usage with acute alcohol and antidepressant treatment. These shared differentially expressed exons may give rise to isoforms and proteins with altered function or localization in the synapse. Some of these differentially expressed exons were identified in genes known to have alternative isoforms with AUD and MDD. These data implicate alternative splicing and isoform expression in the acute antidepressant-like effects of ethanol and the development of comorbid alcohol and depression. Understanding the molecular basis for comorbidity may aid in development of treatment options for afflicted individuals with dual disorders, as well as explore the mechanism for the initiation of addiction with acute exposure to alcohol Advisors/Committee Members: Harris, R. Adron (advisor), Raab-Graham, Kimberly F. (advisor), Golding, Nace (committee member), Morrisett, Richard (committee member), Macdonald, Paul (committee member).

Subjects/Keywords: Alcohol use disorder; Major depressive disorder; Ethanol; Rapid antidepressants; FMRP; GABABR; Ro 25-6981; RNA-sequencing; Synaptoneurosomes; Exon usage

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Wolfe, S. A. (2017). Molecular mechanisms underlying alcohol use disorder and major depressive disorder comorbidity. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://dx.doi.org/10.26153/tsw/2231

Chicago Manual of Style (16^th Edition):

Wolfe, Sarah Anne. “Molecular mechanisms underlying alcohol use disorder and major depressive disorder comorbidity.” 2017. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://dx.doi.org/10.26153/tsw/2231.

MLA Handbook (7^th Edition):

Wolfe, Sarah Anne. “Molecular mechanisms underlying alcohol use disorder and major depressive disorder comorbidity.” 2017. Web. 27 Feb 2021.

Vancouver:

Wolfe SA. Molecular mechanisms underlying alcohol use disorder and major depressive disorder comorbidity. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2017. [cited 2021 Feb 27]. Available from: http://dx.doi.org/10.26153/tsw/2231.

Council of Science Editors:

Wolfe SA. Molecular mechanisms underlying alcohol use disorder and major depressive disorder comorbidity. [Doctoral Dissertation]. University of Texas – Austin; 2017. Available from: http://dx.doi.org/10.26153/tsw/2231

5. Kim, Goheun. Investigating the role of Bruno interactions with oskar regulatory proteins.

Degree: PhD, Cell and Molecular Biology, 2014, University of Texas – Austin

URL: http://hdl.handle.net/2152/31293

► Oskar (Osk) is a posterior body-patterning determinant in Drosophila melanogaster and is highly concentrated at the posterior pole of the oocyte. osk mRNA is translationally… (more)

▼ Oskar (Osk) is a posterior body-patterning determinant in Drosophila melanogaster and is highly concentrated at the posterior pole of the oocyte. osk mRNA is translationally repressed until it reaches the posterior of the oocyte where Osk protein is made. Bruno (Bru) represses translation during osk mRNA localization by direct binding, but how Bru-mediated repression is relieved at the posterior of the oocyte is unknown. Two types of Bru protein interactions are implicated in repression of osk: Bru-Cup interaction and Bru dimerization. By mapping the Bru domains that are important for these interactions, I found that the amino-terminal domain of Bru contributes to both interactions, and deletion of this domain caused a defect in translational repression. However point mutations, within the amino-terminal domain, that disrupt both types of interaction in vitro did not interfere with translational repression in vivo. The difference may be due to other factors stabilizing the Bru-Cup interaction in vivo, as the mutant Bru still associates with Cup in vivo. My work supports the model of repression that relies on Bru interaction with Cup. I also build a new model in which Bru dimerization promotes translational activation of osk, based on my unexpected results: dimerization-defective Bru only weakly accumulated Osk::GFP fusion protein encoded by an osk::GFP reporter RNA bearing a Bru-binding region, while dimerization-competent Bru showed the opposite effect. This suggests that dimerization may contribute to switching Bru from a repressor to an activator, with dimerization controlled via a post-translational modification. Consistent with this, I found that a small fraction of Bru in ovaries is phosphorylated. PKA is a positive regulator of osk expression and phosphorylates Bru in vitro. To test if PKA regulation of osk is mediated through Bru, I examined the effect of altering PKA activity on Bru phosphorylation and Bru-mediated repression. Modulating PKA activity caused small, yet detectable changes in Bru phosphorylation and Bru-dependent translational repression using an osk::GFP reporter. However, while the studies with Bru mutants suggest that phosphorylation promotes repression by Bru, these studies argue for a role in promoting activation. Further work will be required to explain these phenomena. Advisors/Committee Members: Macdonald, Paul M. (advisor), Browning, Karen (committee member), Fischer, Janice (committee member), Stein, David (committee member), Stevens, Scott (committee member).

Subjects/Keywords: Bruno; Oskar; Cup; PKA; Drosophila

11 more images…

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Kim, G. (2014). Investigating the role of Bruno interactions with oskar regulatory proteins. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/31293

Chicago Manual of Style (16^th Edition):

Kim, Goheun. “Investigating the role of Bruno interactions with oskar regulatory proteins.” 2014. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/31293.

MLA Handbook (7^th Edition):

Kim, Goheun. “Investigating the role of Bruno interactions with oskar regulatory proteins.” 2014. Web. 27 Feb 2021.

Vancouver:

Kim G. Investigating the role of Bruno interactions with oskar regulatory proteins. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2014. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/31293.

Council of Science Editors:

Kim G. Investigating the role of Bruno interactions with oskar regulatory proteins. [Doctoral Dissertation]. University of Texas – Austin; 2014. Available from: http://hdl.handle.net/2152/31293

University of Texas – Austin

6. Kanke, Matthew Robert. Characterization of oskar translational activation and the oskar RNA function.

Degree: PhD, Cell and Molecular Biology, 2014, University of Texas – Austin

URL: http://hdl.handle.net/2152/33258

► Oskar (Osk) protein is required for posterior body patterning and establishment of the germline in Drosophila. Coordination of osk mRNA localization and translational regulation ensures… (more)

▼ Oskar (Osk) protein is required for posterior body patterning and establishment of the germline in Drosophila. Coordination of osk mRNA localization and translational regulation ensures Osk protein expression is confined to the oocyte posterior. Proper expression requires repression of osk RNA during transport and activation upon localization. Once activated, osk mRNA is translated into two protein isoforms, Long and Short Osk. Here I describe an element in the 5’ end of osk mRNA that is highly conserved across multiple Drosophila species and required for osk translational activation. This 5’ element is located in a region that is also protein coding for the longer Osk isoform and assays were designed to disentangle the effects that mutations had on protein and RNA function. The 5’ element is needed for efficient Osk translation, but only in the absence of Long Osk translation from the same transcript, suggesting a redundant role. Although the 5’ element was previously implicated in a posterior-specific relief of repression, here I provide evidence that the 5’ element acts as a general enhancer of translation, independent of localization and repression. In addition to its protein coding role, osk mRNA has a non-coding function. Egg chambers lacking osk mRNA fail to form a karyosome and arrest mid-oogenesis. RNA function depends on the presence of the osk 3’ UTR in the oocyte. Here I demonstrate that osk mRNA influences distribution of regulators. In the absence of osk mRNA these regulators dissociate from ribonucleoproteins in the germ cells and accumulate in the follicle cells. I find that the osk 3’ UTR performs multiple roles contributing to RNA function. Multiple binding sites act to sequester the translational repressor Bruno in one role. Another involves sequences not bound by Bruno near the 3’ end of osk. In contrary to disruption of Bruno sequestration, which requires mutation of multiple binding sites, mutation of a single site was sufficient to disrupt RNA function. However, disruption of either role recapitulates the failure of karyosome formation and the accumulation of regulators in the follicle cells. Advisors/Committee Members: Macdonald, Paul M. (advisor), Fischer, Janice (committee member), Johnson, Arlen (committee member), Raab-Graham, Kimberly (committee member), Stein, David (committee member).

Subjects/Keywords: Translation regulation; Drosophila oogenesis; Oskar; RNA function

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Kanke, M. R. (2014). Characterization of oskar translational activation and the oskar RNA function. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/33258

Chicago Manual of Style (16^th Edition):

Kanke, Matthew Robert. “Characterization of oskar translational activation and the oskar RNA function.” 2014. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/33258.

MLA Handbook (7^th Edition):

Kanke, Matthew Robert. “Characterization of oskar translational activation and the oskar RNA function.” 2014. Web. 27 Feb 2021.

Vancouver:

Kanke MR. Characterization of oskar translational activation and the oskar RNA function. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2014. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/33258.

Council of Science Editors:

Kanke MR. Characterization of oskar translational activation and the oskar RNA function. [Doctoral Dissertation]. University of Texas – Austin; 2014. Available from: http://hdl.handle.net/2152/33258

University of Texas – Austin

7. Xie, Xuanhua. Function and regulation of Drosophila Epsin in notch signaling.

Degree: PhD, Cell and Molecular Biology, 2011, University of Texas – Austin

URL: http://hdl.handle.net/2152/ETD-UT-2011-12-4767

► Epsin is an endocytic protein that binds Clathrin, the plasma membrane, Ubiquitin, and also a variety of other endocytic proteins through well-characterized motifs. Although Epsin… (more)

▼ Epsin is an endocytic protein that binds Clathrin, the plasma membrane, Ubiquitin, and also a variety of other endocytic proteins through well-characterized motifs. Although Epsin is a general endocytic factor, genetic analysis in Drosophila and mice revealed that Epsin is essential specifically for internalization of ubiquitinated transmembrane ligands of the Notch receptor, a process required for Notch activation. How Epsin promotes ligand endocytosis and thus Notch signaling is unclear. Here, by generating Drosophila lines containing transgenes that express a variety of different Epsin deletion and substitution variants, I tested each of the five protein or lipid interaction modules of Epsin for a role in Notch activation by each of the two Drosophila ligands, Serrate and Delta. here are five main results of this work that impact present thinking about endocytic machinery/Epsin, Epsin/ligand, or ligand/receptor interactions at the plasma membrane. First, I discovered that deletion or mutation of both UIMs destroys Epsin’s function in Notch signaling and has a greater negative effect on Epsin’s ability to function than removal of any other module type. Second, only one of the two UIMs of Epsin is essential. Third, the lipid-binding function of the ENTH domain is required for maximal Epsin activity. Fourth, although the C-terminal Epsin modules that interact with Clathrin, the adapter protein complex AP-2, or endocytic accessory proteins are necessary collectively for Epsin activity, their functions are highly redundant. Finally, I detected no ligand-specific requirements for Epsin modules. Most unexpected was the finding that Epsin’s Clathrin binding motifs were dispensable. All of these observations are consistent with a model where Epsin’s essential function in ligand cells is to link ubiquitinated Notch ligands to Clathrin-coated vesicles through other Clathrin adapter proteins. Advisors/Committee Members: Fischer, Janice Ann (advisor), Macdonald, Paul M. (committee member), O'Halloran, Theresa J. (committee member), Morgan, Jennifer R. (committee member), Thompson, Wesley J. (committee member).

Subjects/Keywords: Epsin; Endocytosis; Notch signaling

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Xie, X. (2011). Function and regulation of Drosophila Epsin in notch signaling. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/ETD-UT-2011-12-4767

Chicago Manual of Style (16^th Edition):

Xie, Xuanhua. “Function and regulation of Drosophila Epsin in notch signaling.” 2011. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/ETD-UT-2011-12-4767.

MLA Handbook (7^th Edition):

Xie, Xuanhua. “Function and regulation of Drosophila Epsin in notch signaling.” 2011. Web. 27 Feb 2021.

Vancouver:

Xie X. Function and regulation of Drosophila Epsin in notch signaling. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2011. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/ETD-UT-2011-12-4767.

Council of Science Editors:

Xie X. Function and regulation of Drosophila Epsin in notch signaling. [Doctoral Dissertation]. University of Texas – Austin; 2011. Available from: http://hdl.handle.net/2152/ETD-UT-2011-12-4767

8. Geng, Cuiyun. Functional characterization of the role of Imp, a Drosophila mRNA binding protein, during oogenesis.

Degree: PhD, Molecular Biology, 2006, University of Texas – Austin

URL: http://hdl.handle.net/2152/29593

► Establishment of cell polarity requires the involvement of several posttranscriptional regulatory mechanisms, including mRNA localization and translational control. A family of highly conserved RNA binding… (more)

▼ Establishment of cell polarity requires the involvement of several posttranscriptional regulatory mechanisms, including mRNA localization and translational control. A family of highly conserved RNA binding proteins in vertebrates, VICKZ (V̲g1RBP/V̲era, I̲MP-1, 2, 3, C̲RD-BP, K̲OC, Z̲BP-1) proteins, has been shown to act in these two processes. Previous studies of the posttranscriptional mechanisms mediated by VICKZ family members have been largely limited by the lack of genetic approaches in certain vertebrate systems. Identification of Imp, the Drosophila member of the VICKZ family, opened the possibility to use genetic approaches to investigate the roles of a VICKZ family member in mRNA localization and translational control. In this dissertation, we show that Imp is associated with Squid and Hrp48, two heterogeneous proteins (hnRNP) that complex with one another to regulate localized expression of gurken (grk). In addition, Imp binds grk mRNA with high affinity in vitro and is concentrated at the site of grk localization in midstage oocytes. Mutation of the Imp gene does not substantially alter grk expression, but does partially suppress the grk mis-expression phenotype of fs(1)k10 mutants. In contrast, overexpression of Imp in germ line cells results in mislocalization of grk mRNA and protein. The opposing effects of reduced and elevated Imp activities on grk expression suggest that Imp acts in regulation of grk expression, but in a redundant way. To further explore the mechanisms by which localized expression of grk is regulated by Imp, a deficiency screen was conducted to search for dominant modifiers of the dorsalized phenotype resulting from Imp overexpression. Twelve genomic regions were identified to contain dominant modifiers of the Imp overexpression phenotype. Further characterization of mutants of genes within these genomic regions led to identification of five modifiers, including cyclin E (cycE), E2f transcriptional factor 1 (E2f1), lingerer (lig), snail (sna) and mushroom body expressed (mub). E2f1 encodes a transcriptional factor that is involved in regulating the G1 to S phase transition during mitosis. Mutation of E2f1 results in altered grk mRNA and protein distribution within oocyte, revealing a role for this gene in regulation of grk expression. Advisors/Committee Members: Macdonald, Paul M. (advisor).

Subjects/Keywords: Cell polarity; MRNA localization; VICKZ proteins; Imp; MRNA translational control; Drosophila; Binding protein; Oogenesis

11 more images…

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Geng, C. (2006). Functional characterization of the role of Imp, a Drosophila mRNA binding protein, during oogenesis. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/29593

Chicago Manual of Style (16^th Edition):

Geng, Cuiyun. “Functional characterization of the role of Imp, a Drosophila mRNA binding protein, during oogenesis.” 2006. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/29593.

MLA Handbook (7^th Edition):

Geng, Cuiyun. “Functional characterization of the role of Imp, a Drosophila mRNA binding protein, during oogenesis.” 2006. Web. 27 Feb 2021.

Vancouver:

Geng C. Functional characterization of the role of Imp, a Drosophila mRNA binding protein, during oogenesis. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2006. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/29593.

Council of Science Editors:

Geng C. Functional characterization of the role of Imp, a Drosophila mRNA binding protein, during oogenesis. [Doctoral Dissertation]. University of Texas – Austin; 2006. Available from: http://hdl.handle.net/2152/29593

9. Yan, Nan, 1979-. Functional characterization of the role of Bruno protein in translational regulation and germ line development in Drosophila melanogaster.

Degree: PhD, Cell and Molecular Biology, 2006, University of Texas – Austin

URL: http://hdl.handle.net/2152/13084

► Both body axes of the Drosophila egg are determined by localization of several mRNAs to specific regions within the oocyte. One of these mRNAs, oskar… (more)

▼ Both body axes of the Drosophila egg are determined by localization of several mRNAs to specific regions within the oocyte. One of these mRNAs, oskar (osk), is required for posterior body patterning. Localization and translational control are both crucial for the correct deployment of osk. Bruno (Bru) binds specifically to the 3’UTR of the osk mRNA and represses osk translation. In this dissertation, I first describe a genetic screen looking for dominant modifiers of the arrest (aret) mutant phenotype (aret encodes Bru). Two modifiers suggested additional targets for Bru action. One is Star, a gene that contributes to provision of Gurken activity. The second suggested target is a gene acting in the Delta signaling pathway. A final modifier, Lk6, encodes a protein kinase predicted to regulate eIF4E. I also took a biochemical approach trying to understand how Bru regulates osk translation. Bru protein contains three RNA Recognition Motifs, but the remainder of the protein had no known function. I identified a domain, which is required for interaction to Bru itself, Cup and Apontic. Subsequent analysis of mutant forms of Bruno defective in these interactions led us to an unexpected discovery that Bru also acts as an activator of osk translation. Parallel analysis of Bru binding sites in osk 3’UTR fully support the notion that Bru has a dual role. There are two clusters of Bru Recognition Elements in either end of osk 3’UTR. Point mutations in one cluster cause overproduction of Osk protein while point mutations in the other cluster largely prevent translation of the message. To understand the molecular basis of the opposing roles of Bru, I used quantitative methods to better define and compare the binding of Bru to the different regulatory elements: those that either repress or activate osk mRNA translation. Using purified components I found that Bru binds to two clusters of binding sites in the osk 3’UTR differently, in terms of affinity, cooperativity and apparent compaction of the RNA. This work raises the possibility that the details of how Bru binds its substrate may determine whether it acts as a repressor or an activator. Advisors/Committee Members: Macdonald, Paul M. (advisor).

Subjects/Keywords: RNA-protein interactions; Genetic translation; Proteins; Messenger RNA; Drosophila melanogaster

10 more images…

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Yan, Nan, 1. (2006). Functional characterization of the role of Bruno protein in translational regulation and germ line development in Drosophila melanogaster. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/13084

Chicago Manual of Style (16^th Edition):

Yan, Nan, 1979-. “Functional characterization of the role of Bruno protein in translational regulation and germ line development in Drosophila melanogaster.” 2006. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/13084.

MLA Handbook (7^th Edition):

Yan, Nan, 1979-. “Functional characterization of the role of Bruno protein in translational regulation and germ line development in Drosophila melanogaster.” 2006. Web. 27 Feb 2021.

Vancouver:

Yan, Nan 1. Functional characterization of the role of Bruno protein in translational regulation and germ line development in Drosophila melanogaster. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2006. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/13084.

Council of Science Editors:

Yan, Nan 1. Functional characterization of the role of Bruno protein in translational regulation and germ line development in Drosophila melanogaster. [Doctoral Dissertation]. University of Texas – Austin; 2006. Available from: http://hdl.handle.net/2152/13084

10. Bal, Sheila G. Identification of components involved in Epsin ubiquitination.

Degree: MA, Cellular and Molecular Biology, 2012, University of Texas – Austin

URL: http://hdl.handle.net/2152/ETD-UT-2012-08-6140

► Notch signaling is a major signaling pathway that occurs in many tissues at in nearly all stages of development. In Drosophila, Notch and its ligands,… (more)

Subjects/Keywords: Epsin; Ubiquitination

10 more images…

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Bal, S. G. (2012). Identification of components involved in Epsin ubiquitination. (Masters Thesis). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/ETD-UT-2012-08-6140

Chicago Manual of Style (16^th Edition):

Bal, Sheila G. “Identification of components involved in Epsin ubiquitination.” 2012. Masters Thesis, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/ETD-UT-2012-08-6140.

MLA Handbook (7^th Edition):

Bal, Sheila G. “Identification of components involved in Epsin ubiquitination.” 2012. Web. 27 Feb 2021.

Vancouver:

Bal SG. Identification of components involved in Epsin ubiquitination. [Internet] [Masters thesis]. University of Texas – Austin; 2012. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/ETD-UT-2012-08-6140.

Council of Science Editors:

Bal SG. Identification of components involved in Epsin ubiquitination. [Masters Thesis]. University of Texas – Austin; 2012. Available from: http://hdl.handle.net/2152/ETD-UT-2012-08-6140

University of Texas – Austin

11. Jones, Jennifer Rebecca, 1978-. Novel roles of the proteins Oskar and Bluestreak in germ cell formation and migration.

Degree: PhD, Cell and Molecular Biology, 2007, University of Texas – Austin

URL: http://hdl.handle.net/2152/3384

► The formation of germ cells in Drosophila melanogaster is dependent on the presence of ribonucleoprotein complexes called polar granules. A key component of these complexes… (more)

Subjects/Keywords: Germ cells; Nucleoproteins; Cells – Growth; Cell migration; Drosophila melanogaster

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Jones, Jennifer Rebecca, 1. (2007). Novel roles of the proteins Oskar and Bluestreak in germ cell formation and migration. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/3384

Chicago Manual of Style (16^th Edition):

Jones, Jennifer Rebecca, 1978-. “Novel roles of the proteins Oskar and Bluestreak in germ cell formation and migration.” 2007. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/3384.

MLA Handbook (7^th Edition):

Jones, Jennifer Rebecca, 1978-. “Novel roles of the proteins Oskar and Bluestreak in germ cell formation and migration.” 2007. Web. 27 Feb 2021.

Vancouver:

Jones, Jennifer Rebecca 1. Novel roles of the proteins Oskar and Bluestreak in germ cell formation and migration. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2007. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/3384.

Council of Science Editors:

Jones, Jennifer Rebecca 1. Novel roles of the proteins Oskar and Bluestreak in germ cell formation and migration. [Doctoral Dissertation]. University of Texas – Austin; 2007. Available from: http://hdl.handle.net/2152/3384

12. Reich, John Curtis. Determination of how miRNAs mediate repression in Drosophila and the essential role of the oskar mRNA in egg chamber development.

Degree: PhD, Cell and Molecular Biology, 2009, University of Texas – Austin

URL: http://hdl.handle.net/2152/19841

► miRNAs are important regulators of gene expression. These small RNAs function throughout development and regulate translation of a number mRNAs. miRNAs exert their affect on… (more)

▼ miRNAs are important regulators of gene expression. These small RNAs function throughout development and regulate translation of a number mRNAs. miRNAs exert their affect on translation as part of the RNP complex RISC. RISC can affect translation of transcripts at both the level of translation initiation, and post-initiation. Although mechanisms of repression mediated by miRNAs have been intensively studied, repression is not well characterized. In order to understand how miRNAs regulate translation in Drosophila, we first characterized miRNA-mediated repression in the ovary. We developed an ovarian assay sensitive to regulation by miRNAs and found that regulated transcripts localize to cytoplasmic puncta distinct from sponge bodies, cytoplasmic RNP structures consisting of proteins implicated in miRNA-mediated regulation. In addition, we devised a genetic screen to identify genes involved in miRNA-mediated regulation. Seven mutants were isolated from the screen, and two mutants were subsequently mapped to separate 1Mb genomic regions. Both these regions are devoid of genes implicated in miRNA-mediated regulation, suggesting our mutants identify novel components involved in repression. The oskar mRNA encodes for the Oskar protein, which is vital in establishing the posterior axis of the Drosophila embryo. In addition to its protein coding function, the osk mRNA has another essential role: it is required for egg chamber progression through oogenesis. This role of oskar is mediated by its 3ʼ UTR, but how it functions in this role is unknown. Here, we investigate the function of the 3ʼ UTR and discover that the well-defined BRE sequences are required for egg chamber progression through oogenesis. The BREs mediate translational repression of the highly regulated oskar mRNA and were previously defined by their ability to bind Bruno, which represses translation of the oskar mRNA. We also provide evidence that the osk BREs sequester Bruno, potentially inhibiting Bruno from binding and misregulating other mRNAs. Our results suggest a novel regulatory loop, where oskar sequesters and inhibits Bruno from misregulating mRNAs, and Bruno, in turn, regulates translation of the oskar mRNA. Advisors/Committee Members: Macdonald, Paul M. (advisor), Fischer, Janice (committee member), Stein, David (committee member), Sullivan, Christopher (committee member), Gross, Jeffrey (committee member).

Subjects/Keywords: miRNA; Drosophila; Oskar

10 more images…

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Reich, J. C. (2009). Determination of how miRNAs mediate repression in Drosophila and the essential role of the oskar mRNA in egg chamber development. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/19841

Chicago Manual of Style (16^th Edition):

Reich, John Curtis. “Determination of how miRNAs mediate repression in Drosophila and the essential role of the oskar mRNA in egg chamber development.” 2009. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/19841.

MLA Handbook (7^th Edition):

Reich, John Curtis. “Determination of how miRNAs mediate repression in Drosophila and the essential role of the oskar mRNA in egg chamber development.” 2009. Web. 27 Feb 2021.

Vancouver:

Reich JC. Determination of how miRNAs mediate repression in Drosophila and the essential role of the oskar mRNA in egg chamber development. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2009. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/19841.

Council of Science Editors:

Reich JC. Determination of how miRNAs mediate repression in Drosophila and the essential role of the oskar mRNA in egg chamber development. [Doctoral Dissertation]. University of Texas – Austin; 2009. Available from: http://hdl.handle.net/2152/19841

13. Banks, Susan Marie-Louise. The role of auxilin and endocytosis in delta signaling.

Degree: PhD, Cell and Molecular Biology, 2012, University of Texas – Austin

URL: http://hdl.handle.net/2152/ETD-UT-2012-05-5372

► Notch signaling is important for cell-cell signaling during development. Notch signaling is highly conserved across all metazoans and failure in Notch signaling is causative in… (more)

▼ Notch signaling is important for cell-cell signaling during development. Notch signaling is highly conserved across all metazoans and failure in Notch signaling is causative in many human diseases. In the Drosophila eye, activation of the Notch pathway requires Lqf (Drosophila Epsin)-dependent and Clathrin-dependent internalization of the Notch receptor ligands, Delta or Serrate, by the signal-sending cells. However, it is unclear why ligand must be internalized into the signal-sending cells to activate Notch signaling in the signal-receiving cells. Evidence suggests that in addition to Clathrin and Epsin, Auxilin is essential for signaling and is indirectly required for internalization of the Notch receptor ligand Delta. Auxilin functions in uncoating Clathrin-coated vesicles to maintain a pool of free Clathrin and Epsin in the cell. auxilin mutants were used as an entryway to identify previously unknown components of the Notch signaling pathway. An F1, FLP/FRT, EMS screen was performed and enhancers of an auxilin mutant rough eye defect were isolated. The enhancers ultimately formed one complementation group on the 2nd chromosome and fourteen complementation groups on the 3rd chromosome. Three of the 3rd chromosome complementation groups were each identified as Delta, lqf, or hsc70. A single allele was identified as faf. Delta and Epsin have known roles in signaling cells to activate Notch as described above. Hsc70 is an ATPase that functions with Auxilin to uncoat Clathrin-coated vesicles and Faf is a deubiquitinating enzyme that maintains levels of active Epsin in the cell. These results suggest I have isolated mutations in genes closely tied to Notch signaling or functioning directly with Auxilin. Mutations in two genes previously undescribed in Notch signaling in the developing Drosophila eye were also isolated from the screen and identified. The second chromosome complementation group was identified as α-adaptin. α-Adaptin is a subunit of the heterotetrameric Clathrin adaptor protein AP-2. One of the third chromosome complementation groups was identified as crumbs. Crumbs is an integral membrane protein that functions at adherens junctions and in establishing apical/basal polarity in cells. Characterizing roles for α-Adaptin and Crumbs during Notch signaling may elucidate the purpose for Delta internalization to activate Notch signaling. Advisors/Committee Members: Fischer, Janice Ann (advisor), Huibregtse, Jon (committee member), Macdonald, Paul (committee member), Morgan, Jennifer (committee member), O'Halloran, Theresa (committee member).

Subjects/Keywords: Notch; Delta; Endocytosis; Epsin; Lqf; Auxilin; Clathrin; Faf; Hsc70; AP-2; Crumbs

10 more images…

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Banks, S. M. (2012). The role of auxilin and endocytosis in delta signaling. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/ETD-UT-2012-05-5372

Chicago Manual of Style (16^th Edition):

Banks, Susan Marie-Louise. “The role of auxilin and endocytosis in delta signaling.” 2012. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/ETD-UT-2012-05-5372.

MLA Handbook (7^th Edition):

Banks, Susan Marie-Louise. “The role of auxilin and endocytosis in delta signaling.” 2012. Web. 27 Feb 2021.

Vancouver:

Banks SM. The role of auxilin and endocytosis in delta signaling. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2012. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/ETD-UT-2012-05-5372.

Council of Science Editors:

Banks SM. The role of auxilin and endocytosis in delta signaling. [Doctoral Dissertation]. University of Texas – Austin; 2012. Available from: http://hdl.handle.net/2152/ETD-UT-2012-05-5372

14. White, Travis Brandon. Group II intron and gene targeting reactions in Drosophila melanogaster.

Degree: PhD, Cell and Molecular Biology, 2011, University of Texas – Austin

URL: http://hdl.handle.net/2152/ETD-UT-2011-08-4052

► Mobile group II introns are retroelements that insert site-specifically into double-stranded DNA sites by a process called retrohoming. Retrohoming activity rests in a ribonucleoprotein (RNP)… (more)

▼ Mobile group II introns are retroelements that insert site-specifically into double-stranded DNA sites by a process called retrohoming. Retrohoming activity rests in a ribonucleoprotein (RNP) complex that contains an intron-encoded protein (IEP) and the excised intron RNA. The intron RNA uses its ribozyme activity to reverse splice into the top strand of the DNA target site, while the IEP cleaves the bottom DNA strand and reverse transcribes the inserted intron. My dissertation focuses on the Lactococcus lactis Ll.LtrB group II intron and its IEP, denoted LtrA. First, I investigated the ability of microinjected Ll.LtrB RNPs to retrohome into plasmid target sites in Drosophila melanogaster precellular blastoderm stage embryos. I found that injection of extra Mg2+ into the embryo was crucial for efficient retrohoming. Next, I compared retrohoming of linear and lariat forms of the intron RNP. Unlike lariat RNPs, retrohoming products of linear intron RNPs displayed heterogeneity at the 5’-intron insertion junction, including 5’-exon resection, intron truncation, and/or repair at regions of microhomology. To investigate whether these junctions result from cDNA ligation by non-homologous end-joining (NHEJ), I analyzed retrohoming of linear and lariat intron RNPs in D. melanogaster embryos with null mutations in the NHEJ genes lig4 and ku70, as well as the DNA repair polymerase polQ. I found that null mutations in each gene decreased retrohoming of linear compared to lariat intron RNPs. To determine whether novel activities of the LtrA protein contributed to the linear intron retrohoming 5’ junctions, I assayed the polymerase, non-templated nucleotide addition and template-switching activities of LtrA on oligonucleotide substrates mimicking the 5’-intron insertion junction in vitro. Although LtrA efficiently template switched to 5’-exon DNA substrates, the junctions produced differed from those observed in vivo, indicating that template switching is not a significant alternative to NHEJ in vivo. Finally, I designed and constructed retargeted Ll.LtrB RNPs to site-specifically insert into endogenous chromosomal DNA sites in D. melanogaster. I obtained intron integration efficiencies into chromosomal targets up to 0.4% in embryos and 0.021% in adult flies. These studies expand the utility of group II intron RNPs as gene targeting tools in model eukaryotic organisms. Advisors/Committee Members: Lambowitz, Alan (advisor), Bull, James J. (committee member), Macdonald, Paul M. (committee member), Paull, Tanya T. (committee member), Stevens, Scott W. (committee member).

Subjects/Keywords: Catalytic RNA; Group II introns; Reverse transcriptases; Gene targeting; Drosophila

10 more images…

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

White, T. B. (2011). Group II intron and gene targeting reactions in Drosophila melanogaster. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/ETD-UT-2011-08-4052

Chicago Manual of Style (16^th Edition):

White, Travis Brandon. “Group II intron and gene targeting reactions in Drosophila melanogaster.” 2011. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/ETD-UT-2011-08-4052.

MLA Handbook (7^th Edition):

White, Travis Brandon. “Group II intron and gene targeting reactions in Drosophila melanogaster.” 2011. Web. 27 Feb 2021.

Vancouver:

White TB. Group II intron and gene targeting reactions in Drosophila melanogaster. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2011. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/ETD-UT-2011-08-4052.

Council of Science Editors:

White TB. Group II intron and gene targeting reactions in Drosophila melanogaster. [Doctoral Dissertation]. University of Texas – Austin; 2011. Available from: http://hdl.handle.net/2152/ETD-UT-2011-08-4052

15. Cho, Yong Suk, 1970-. Studies of the regulation of serine protease activity in the establishment of the dorsal-ventral axis of the Drosophila embryo.

Degree: PhD, Cell and Molecular Biology, 2010, University of Texas – Austin

URL: http://hdl.handle.net/2152/ETD-UT-2010-05-992

► Dorsal-ventral (DV) polarity in the Drosophila embryo is defined by spatially regulated activation of the transmembrane receptor Toll, which is uniformly distributed throughout the early… (more)

▼ Dorsal-ventral (DV) polarity in the Drosophila embryo is defined by spatially regulated activation of the transmembrane receptor Toll, which is uniformly distributed throughout the early embryo's plasma membrane. Ventral activation of Toll is accomplished through the local production of its activating ligand, a processed C-terminal fragment of the Spätzle protein, which is generated in the last step of a proteolytic cascade involving the sequentially-acting proteases Gastrulation Defective (GD), Snake and Easter. Pipe protein, a homologue of vertebrate glycosaminoglycan modifying enzymes, which is expressed during oogenesis in ventral follicle cells adjacent to the developing oocyte, is believed to control the ventrally restricted processing of Spätzle. pipe expression and the sulfation of its enzymatic target in the ventral follicle cells leads to the formation of a stable ventral cue, embedded in the eggshell. Recently the Pipe enzymatic target has been identified as several protein components of the vitelline membrane, the inner layer of the eggshell. Prior to this work, an important piece of information missing from our understanding of Drosophila DV patterning was the identity of the initial step in the protease cascade that requires Pipe activity. Here, I show that the processing of Snake is independent of Pipe activity, while the processing of Easter requires Pipe function, indicating that Easter processing by Snake is the key proteolytic step that is controlled by Pipe activity and presumably the first cleavage event that is spatially regulated. A second key gap in our understanding of Drosophila embryonic DV patterning concerned the role of GD in the protease cascade. While GD is the protease that cleaves and activates Snake, the existence of two distinct classes of complementing gd alleles has suggested that GD provides another, distinct function. Investigations described here indicate that the second function of GD is to promote the ability of activated Snake to process Easter, independent of its Snake-processing function. Finally, I provide evidence for the formation of protein complexes containing various components of the serine protease cascade, which suggest that conformational changes in the complexes, which act to promote productive interactions between the proteins, are an important aspect of their activation. Advisors/Committee Members: Stein, David S. (advisor), Agarwala, Seema (committee member), Fischer, Janice A. (committee member), Macdonald, Paul M. (committee member), O'Halloran, Theresa J. (committee member).

Subjects/Keywords: Drosophila; Axis establishment; Pipe; Serine protease; Drosophila embryo; Dorsal-ventral polarity; Toll receptor; Spätzle protein; Gastrulation Defective

10 more images…

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Cho, Yong Suk, 1. (2010). Studies of the regulation of serine protease activity in the establishment of the dorsal-ventral axis of the Drosophila embryo. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/ETD-UT-2010-05-992

Chicago Manual of Style (16^th Edition):

Cho, Yong Suk, 1970-. “Studies of the regulation of serine protease activity in the establishment of the dorsal-ventral axis of the Drosophila embryo.” 2010. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/ETD-UT-2010-05-992.

MLA Handbook (7^th Edition):

Cho, Yong Suk, 1970-. “Studies of the regulation of serine protease activity in the establishment of the dorsal-ventral axis of the Drosophila embryo.” 2010. Web. 27 Feb 2021.

Vancouver:

Cho, Yong Suk 1. Studies of the regulation of serine protease activity in the establishment of the dorsal-ventral axis of the Drosophila embryo. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2010. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/ETD-UT-2010-05-992.

Council of Science Editors:

Cho, Yong Suk 1. Studies of the regulation of serine protease activity in the establishment of the dorsal-ventral axis of the Drosophila embryo. [Doctoral Dissertation]. University of Texas – Austin; 2010. Available from: http://hdl.handle.net/2152/ETD-UT-2010-05-992

16. Wang, Howard. Examining the role of Golgi-associated protein, Lava lamp, in Drosophila development.

Degree: PhD, Cell and Molecular Biology, 2010, University of Texas – Austin

URL: http://hdl.handle.net/2152/ETD-UT-2010-05-1024

► The Golgi body is responsible for the modification and sorting of proteins and lipids in the secretory pathway. The Golgi must coordinate with other endomembrane… (more)

▼ The Golgi body is responsible for the modification and sorting of proteins and lipids in the secretory pathway. The Golgi must coordinate with other endomembrane compartments in order to target cargo to the correct destination. While our understanding of Golgi function is vast, we can extend our knowledge base by examining the functions of Golgi-associated proteins in developing animals. Lava lamp (Lva) is a Golgi-associated protein and a Drosophila golgin. Previously, Lva was shown to facilitate efficient membrane secretion required for cleavage furrow formation in early embryos. By acting as an adaptor molecule between Golgi and microtubule motility factors, Lva is thought to position Golgi bodies for targeted secretion during cellularization, the Drosophila cleavage stage of development. Here, I further characterize the role of Lva during animal development. I demonstrate that Lva is required for animal viability, and gamete production in females but not males. While Lva is expressed in many tissues, adult fat body cells are the most sensitive to decreased Lva activity, resulting in the disorganization of endomembrane compartments. Furthermore, this disruption in adult fat body cells correlates with a defect in neuroendocrine signaling, altering the activity of juvenile hormone. I propose that Lva activity in adult fat body cells is important for recognizing and/or processing juvenile hormone in order to support Drosophila oogenesis. Lva’s role in cellularization, which is a specialized form of cytokinesis in early embryos, provided insights into the combined processes of actomyosin-based contraction and membrane secretion. While some proteins have been implicated in cellularization, there are thought to be many more that have yet to be identified. In an effort to isolate additional genes involved in animal cell cytokinesis, we screened a unique collection of temperature sensitive (ts) mutations on the X-chromosome of Drosophila melanogaster. At the restrictive temperature, we identified five mutants that displayed a cellularization phenotype. For one of the mutants, fs(1)ts242, we narrowed the mutation to a region on the X chromosome consisting of 17 possible gene candidates. Identification of the gene should provide further elucidation of the mechanisms controlling actomyosin-based contraction and membrane secretion. Advisors/Committee Members: Macdonald, Paul M. (advisor), Sisson, John Charles (advisor), O'Halloran, Terry J. (committee member), Stein, David (committee member), Thompson, Wesley J. (committee member), De Lozanne, Arturo (committee member).

Subjects/Keywords: Golgi; Golgin; Juvenile hormone; Oogenesis; Cellularization

1 more image…

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Wang, H. (2010). Examining the role of Golgi-associated protein, Lava lamp, in Drosophila development. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/ETD-UT-2010-05-1024

Chicago Manual of Style (16^th Edition):

Wang, Howard. “Examining the role of Golgi-associated protein, Lava lamp, in Drosophila development.” 2010. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/ETD-UT-2010-05-1024.

MLA Handbook (7^th Edition):

Wang, Howard. “Examining the role of Golgi-associated protein, Lava lamp, in Drosophila development.” 2010. Web. 27 Feb 2021.

Vancouver:

Wang H. Examining the role of Golgi-associated protein, Lava lamp, in Drosophila development. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2010. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/ETD-UT-2010-05-1024.

Council of Science Editors:

Wang H. Examining the role of Golgi-associated protein, Lava lamp, in Drosophila development. [Doctoral Dissertation]. University of Texas – Austin; 2010. Available from: http://hdl.handle.net/2152/ETD-UT-2010-05-1024

University of Texas – Austin

17. Reveal, Bradley Steven. Bruno regulates mRNA translation by binding to multiple sequence motifs.

Degree: PhD, Cell and Molecular Biology, 2010, University of Texas – Austin

URL: http://hdl.handle.net/2152/ETD-UT-2010-08-1853

► Oskar (Osk) is a posterior body patterning determinant in Drosophila melanogaster oocytes. oskar (osk) mRNA is translationally repressed until it reaches the posterior of the… (more)

▼ Oskar (Osk) is a posterior body patterning determinant in Drosophila melanogaster oocytes. oskar (osk) mRNA is translationally repressed until it reaches the posterior of the oocyte where Osk protein accumulates. Translational repression of osk prior to posterior localization is mediated by the RNA binding protein, Bruno (Bru). To better define Bru binding sites, I performed in vitro selections using full length Bru and the fragments containing either the first two RRMs (RRM1+2) or the third RRM (RRM3+). The aptamers from the final round from each of the selections produced a multitude of overrepresented primary sequence motifs. Examples of each of these motifs were found in the 3’UTRs of the mRNAs that Bru is known to regulate during oogenesis. GFP reporter transgenes under the control of the UAS-Gal4 expression system were constructed with each class of the binding sites within the reporter transgenes’ 3’UTRs to test the motifs’ ability to repress the reporters in vivo. In a wildtype background, the GFP reporters containing the binding sites were translationally repressed. In the aret mutant background, the GFP levels of the repressed GFP reporters increased with reduced Bru activity, suggesting the transgenes’ repression is mediated by Bru. Three of the motifs isolated in the in vitro selections reside in the AB and C regions of the osk 3’UTR, and the three classes of sites were mutated in the AB and C regions. The mutated AB and C regions were used to assay for a reduction of Bru binding affinity for the mutant RNAs. Additionally, the mutations were incorporated into an osk genomic transgene that was introduced into an osk RNA null as well as an Osk protein null background. The mutations reduced Bru binding to the AB and C regions. The transgenes containing the mutated Bru binding sites could not fully rescue the osk RNA null phenotype but can fully rescue the Osk protein null phenotype, suggesting an osk transcript can regulate other osk mRNAs in trans. Advisors/Committee Members: Macdonald, Paul M. (advisor), Fischer, Janice (committee member), Russell, Rick (committee member), Stein, Dave (committee member), Stevens, Scott (committee member).

Subjects/Keywords: RRM protein; Oskar; Bruno; RNA binding protein

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Reveal, B. S. (2010). Bruno regulates mRNA translation by binding to multiple sequence motifs. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/ETD-UT-2010-08-1853

Chicago Manual of Style (16^th Edition):

Reveal, Bradley Steven. “Bruno regulates mRNA translation by binding to multiple sequence motifs.” 2010. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/ETD-UT-2010-08-1853.

MLA Handbook (7^th Edition):

Reveal, Bradley Steven. “Bruno regulates mRNA translation by binding to multiple sequence motifs.” 2010. Web. 27 Feb 2021.

Vancouver:

Reveal BS. Bruno regulates mRNA translation by binding to multiple sequence motifs. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2010. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/ETD-UT-2010-08-1853.

Council of Science Editors:

Reveal BS. Bruno regulates mRNA translation by binding to multiple sequence motifs. [Doctoral Dissertation]. University of Texas – Austin; 2010. Available from: http://hdl.handle.net/2152/ETD-UT-2010-08-1853

University of Texas – Austin

18. Monzo, Kate Frances. The role of Fragile X mental retardation protein in Drosophila cleavage furrow formation.

Degree: PhD, Cell and Molecular Biology, 2009, University of Texas – Austin

URL: http://hdl.handle.net/2152/ETD-UT-2009-12-411

► Reduced activity of Fragile X mental retardation protein (FMRP) in brain neurons results in the most common form of heritable mental retardation in humans, Fragile… (more)

▼ Reduced activity of Fragile X mental retardation protein (FMRP) in brain neurons results in the most common form of heritable mental retardation in humans, Fragile X Syndrome (FXS). FMRP is a selective RNA-binding protein that is implicated in the translational regulation of specific mRNAs in neurons. Although very few direct targets of FMRP have been identified and verified in vivo, FXS is thought to result from the aberrant regulation of potentially hundreds of mRNAs causing defects in neuron morphology and synapse function. Identifying additional targets will be important for elucidating the mechanism of FMRP regulation as well as the etiology of FXS. Drosophila melanogaster offers a unique and powerful system for studying the function of FMRP. Flies with loss of FMRP activity have neuronal and behavioral defects similar to those observed in humans with FXS. Importantly, FMRP regulates common target mRNAs in neurons in both mice and flies. Here, I will describe our discovery of a previously unknown requirement for Drosophila FMRP (dFMRP) during the cleavage stage of early embryonic development. First, we identified a requirement for dFMRP for proper cleavage furrow formation and found that dFMRP functions to regulate the expression of specific target mRNAs during the cleavage stage. Among these is trailer hitch (tral) mRNA, which encodes a translational regulator as well, and represents a new in vivo target of dFMRP translational regulation. In addition, I have identified twenty-eight proteins that change in expression in the absence of dFMRP using a comparative proteomics based screen for dFMRP targets. One of these is the Chaperonin containing tcp-1 complex (CCT), a previously unidentified target, which I found is itself also required for cleavage furrow formation. Finally, we have identified a new dFMRP protein-binding partner, Caprin, and found that together dFMRP and Caprin are required for the proper timing of the MBT. This set of work has led to a better understanding of the mechanism of dFMRP-dependent regulation of cellular morphogenesis in early embryos and has the potential to lead to a better understanding of the etiology of FXS. Advisors/Committee Members: Sisson, John Charles (advisor), Macdonald, Paul M. (advisor), Fischer, Janice A. (committee member), Johnson, Arlen W. (committee member), Wallingford, John B. (committee member).

Subjects/Keywords: Fragile X Syndrome; Fragile X mental retardation protein; Drosophila; Cleavage; Cellularization

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Monzo, K. F. (2009). The role of Fragile X mental retardation protein in Drosophila cleavage furrow formation. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/ETD-UT-2009-12-411

Chicago Manual of Style (16^th Edition):

Monzo, Kate Frances. “The role of Fragile X mental retardation protein in Drosophila cleavage furrow formation.” 2009. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/ETD-UT-2009-12-411.

MLA Handbook (7^th Edition):

Monzo, Kate Frances. “The role of Fragile X mental retardation protein in Drosophila cleavage furrow formation.” 2009. Web. 27 Feb 2021.

Vancouver:

Monzo KF. The role of Fragile X mental retardation protein in Drosophila cleavage furrow formation. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2009. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/ETD-UT-2009-12-411.

Council of Science Editors:

Monzo KF. The role of Fragile X mental retardation protein in Drosophila cleavage furrow formation. [Doctoral Dissertation]. University of Texas – Austin; 2009. Available from: http://hdl.handle.net/2152/ETD-UT-2009-12-411

University of Texas – Austin

19. Lyon, Angeline Marie. Biophysical studies of an expanded RNA recognition motif from the Bruno protein.

Degree: PhD, Biochemistry, 2009, University of Texas – Austin

URL: http://hdl.handle.net/2152/ETD-UT-2009-08-229

► RNA recognition motifs (RRMs) are a ubiquitous class of proteins which bind RNA in a sequence-specific fashion, often with high affinity. The mechanisms through which… (more)

Subjects/Keywords: Bruno; Oskar; Bruno protein; RNA recognition motif; RRM; RRM domain; NMR; Solution structure; RNA binding; N-terminal residue

Record Details Similar Records Cite « Share

❌

APA · Chicago · MLA · Vancouver · CSE | Export to Zotero / EndNote / Reference Manager

APA (6^th Edition):

Lyon, A. M. (2009). Biophysical studies of an expanded RNA recognition motif from the Bruno protein. (Doctoral Dissertation). University of Texas – Austin. Retrieved from http://hdl.handle.net/2152/ETD-UT-2009-08-229

Chicago Manual of Style (16^th Edition):

Lyon, Angeline Marie. “Biophysical studies of an expanded RNA recognition motif from the Bruno protein.” 2009. Doctoral Dissertation, University of Texas – Austin. Accessed February 27, 2021. http://hdl.handle.net/2152/ETD-UT-2009-08-229.

MLA Handbook (7^th Edition):

Lyon, Angeline Marie. “Biophysical studies of an expanded RNA recognition motif from the Bruno protein.” 2009. Web. 27 Feb 2021.

Vancouver:

Lyon AM. Biophysical studies of an expanded RNA recognition motif from the Bruno protein. [Internet] [Doctoral dissertation]. University of Texas – Austin; 2009. [cited 2021 Feb 27]. Available from: http://hdl.handle.net/2152/ETD-UT-2009-08-229.

Council of Science Editors:

Lyon AM. Biophysical studies of an expanded RNA recognition motif from the Bruno protein. [Doctoral Dissertation]. University of Texas – Austin; 2009. Available from: http://hdl.handle.net/2152/ETD-UT-2009-08-229

		in
And / Or
		in
And / Or
		in
And / Or
		in

Open Access Theses and Dissertations