subject:(Moesin)

University of Alberta

1. Yang, Yang. Flapwing Dephosphorylates Merlin and Moesin and Regulates Epithelial Integrity in Drosophila.

Degree: MS, Department of Cell Biology, 2013, University of Alberta

URL: https://era.library.ualberta.ca/files/vq27zp42z

► Merlin is a tumor suppressor protein whose inactivation is associated with familial Neurofibromatosis Type II (NF2) and other sporadic tumors. The growth-suppressive function of Merlin… (more)

Subjects/Keywords: Merlin; Moesin; epithelial integrity; dephosphorylation; Drosophila; flapwing

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APA (6^th Edition):

Yang, Y. (2013). Flapwing Dephosphorylates Merlin and Moesin and Regulates Epithelial Integrity in Drosophila. (Masters Thesis). University of Alberta. Retrieved from https://era.library.ualberta.ca/files/vq27zp42z

Chicago Manual of Style (16^th Edition):

Yang, Yang. “Flapwing Dephosphorylates Merlin and Moesin and Regulates Epithelial Integrity in Drosophila.” 2013. Masters Thesis, University of Alberta. Accessed January 16, 2021. https://era.library.ualberta.ca/files/vq27zp42z.

MLA Handbook (7^th Edition):

Yang, Yang. “Flapwing Dephosphorylates Merlin and Moesin and Regulates Epithelial Integrity in Drosophila.” 2013. Web. 16 Jan 2021.

Vancouver:

Yang Y. Flapwing Dephosphorylates Merlin and Moesin and Regulates Epithelial Integrity in Drosophila. [Internet] [Masters thesis]. University of Alberta; 2013. [cited 2021 Jan 16]. Available from: https://era.library.ualberta.ca/files/vq27zp42z.

Council of Science Editors:

Yang Y. Flapwing Dephosphorylates Merlin and Moesin and Regulates Epithelial Integrity in Drosophila. [Masters Thesis]. University of Alberta; 2013. Available from: https://era.library.ualberta.ca/files/vq27zp42z

Boston University

2. Engblom, Nels. An investigation into the mechanism of TMIGD1-mediated signal transduction pathway in human epithelial cells.

Degree: MS, Medical Sciences, 2017, Boston University

URL: http://hdl.handle.net/2144/23704

► Dysregulation of protein expression, in particular expression of proto-oncogenes and tumor-suppressor genes whose function play key roles in cell growth, adhesion and migration, are hallmarks… (more)

▼ Dysregulation of protein expression, in particular expression of proto-oncogenes and tumor-suppressor genes whose function play key roles in cell growth, adhesion and migration, are hallmarks of human malignancies. Transmembrane and immunoglobulin-containing domain 1 (TMIGD1) was recently discovered as a cell adhesion molecule (CAM) that plays an important role in epithelial cell function by regulating epithelial cell polarity and adhesion. The extracellular domain of TMIGD1 contains two Ig domains that are involved in cell-cell interaction, followed by a transmembrane region and short cytoplasmic domain with potential to relay signal transduction. Our further investigation demonstrated TMIGD1 is downregulated in human colon cancer, suggesting a potentially important role for TMIGD1 in the regulation colorectal cancer. However, the molecular mechanisms of TMIGD1-mediated signal transduction, which could relay its function in epithelial cells, are not known. Using liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis, we have identified moesin as a possible TMIGD1 binding protein. Moesin, a member of the Ezrin/Radixin/Moesin (ERM) family of proteins, is upregulated in human tumors. Moesin stimulates cell migration, tumor invasion, adherence and modulates cytoskeletal actin assembly. Similar to other ERM family proteins, moesin contains an N-terminal FERM domain, which binds to transmembrane proteins, and a C-terminal C-ERMAD domain, which binds F-actin. The overall goal of this study was to determine the binding of moesin with TMIGD1 and the specific domain involved in mediating the binding of moesin with TMIGD1. Our study in vitro and in vivo binding assays demonstrate that moesin interacts with the cytoplasmic domain of TMIGD1 via its FERM domain. Moreover, we demonstrate TMIGD1 interaction with moesin inhibits phosphorylation of moesin, indicating that perhaps TMIGD1 inhibits tumor cell migration through inhibition of phosphorylation of moesin. Additionally, TMIGD1 alters cellular localization of moesin, suggesting that altered cellular localization by TMIGD1 could account for inhibition of phosphorylation of moesin. We propose that TMIGD1 sequesters moesin near the cell membrane, preventing its interaction with PIP2, which is required for its phosphorylation and hence inhibits moesin activation. Altogether, the data presented in this work identifies moesin as a key signaling component of TMIGD1. Moesin directly interacts with TMIGD1 via its FERM domain. Recruitment of moesin to TMIGD1 blocks phosphorylation of moesin, suggesting that TMIGD1 exerts its effect in tumor cells in part by inhibition of moesin activation.

Subjects/Keywords: Molecular biology; TMIGD1; Cancer; Cell adhesion molecule; Epithelial cells; Moesin

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

APA (6^th Edition):

Engblom, N. (2017). An investigation into the mechanism of TMIGD1-mediated signal transduction pathway in human epithelial cells. (Masters Thesis). Boston University. Retrieved from http://hdl.handle.net/2144/23704

Chicago Manual of Style (16^th Edition):

Engblom, Nels. “An investigation into the mechanism of TMIGD1-mediated signal transduction pathway in human epithelial cells.” 2017. Masters Thesis, Boston University. Accessed January 16, 2021. http://hdl.handle.net/2144/23704.

MLA Handbook (7^th Edition):

Engblom, Nels. “An investigation into the mechanism of TMIGD1-mediated signal transduction pathway in human epithelial cells.” 2017. Web. 16 Jan 2021.

Vancouver:

Engblom N. An investigation into the mechanism of TMIGD1-mediated signal transduction pathway in human epithelial cells. [Internet] [Masters thesis]. Boston University; 2017. [cited 2021 Jan 16]. Available from: http://hdl.handle.net/2144/23704.

Council of Science Editors:

Engblom N. An investigation into the mechanism of TMIGD1-mediated signal transduction pathway in human epithelial cells. [Masters Thesis]. Boston University; 2017. Available from: http://hdl.handle.net/2144/23704

University of Illinois – Chicago

3. Liu, Xiaowen. The ‘Go’ and ‘Stop’ Mechanisms for Neutrophil Migration.

Degree: 2013, University of Illinois – Chicago

URL: http://hdl.handle.net/10027/10374

► Chemotaxis, or directed cell migration is essential for host defense, embryonic development, axon guidance, and tumor invasion. Chemotactic cells such as blood neutrophils and neutrophil-like,… (more)

▼ Chemotaxis, or directed cell migration is essential for host defense, embryonic development, axon guidance, and tumor invasion. Chemotactic cells such as blood neutrophils and neutrophil-like, differentiated HL60 cells respond to a gradient of chemoattractant, e.g., fMet-Leu-Phe (fMLP), by adopting polarized morphology (polarization) and crawling up the gradient (directional sensing). How chemotactic cells initiate polarization and orient their polarity precisely toward spatial cues remains unclear. ‘Global inhibitors’ have been postulated to restrict cells from polarizing in random directions, but only permit the direction pointing to spatial cues. we found that moesin, a cross-linker between plasma membrane and actin cytoskeleton, acted as a global inhibitor for neutrophil chemotaxis, which turned-off both ‘frontness’ and ‘backness’ signals (responsible for pseudopod and uropod formation, respectively), and ensured cell's pseudopod correctly orienting toward the source of attractant in a gradient. Removal of moesin not only enhanced small Rho GTPases, Rac, Rho and Cdc42 activities, but also induced cell protrusion in wrong directions, thus abolished cell’s directional sensing. Myosin phosphatase, on the other hand initiated cell migration by breaking down the global inhibition provided by moesin. In order to kill invading bacteria, neutrophils must interpret spatial cues, migrate, and reach target sites. In addition to mechanisms that promote chemotaxis, there are inhibitory mechanisms ensure chemotactic cells to reach correct destinations where they perform bactericidal functions for phagocytes and antigen identification for homing lymphocytes. To date, little is known about the regulatory mechanisms that inhibit cell migration. We show that two mitogen-activated protein kinases played opposing roles in neutrophil trafficking. The extracellular signal-regulated kinase (Erk) potentiated G protein-coupled receptor kinase GRK2 activity and inhibited neutrophil migration, whereas p38 MAPK acted as a non-canonical GRK that phosphorylated the formyl peptide receptor FPR1 and facilitated neutrophil migration by blocking GRK2 function. Therefore, the dynamic balance between Erk and p38 MAPK controls neutrophil “stop” and “go” behaviors, ensuring neutrophils precisely reach their final destination as the first line of host-defense. Advisors/Committee Members: Minshall, Richard D. (advisor), Xu, Jingsong (committee member), Carnegie, Graeme K. (committee member), Fukai, Torhu (committee member), Lau, Lester F. (committee member), Zhao, Youyang (committee member).

Subjects/Keywords: chemotaxis; moesin; global inhibitor; myosin phosphatase; MAPKs; GRK2; internalization; FPR1

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APA (6^th Edition):

Liu, X. (2013). The ‘Go’ and ‘Stop’ Mechanisms for Neutrophil Migration. (Thesis). University of Illinois – Chicago. Retrieved from http://hdl.handle.net/10027/10374

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Liu, Xiaowen. “The ‘Go’ and ‘Stop’ Mechanisms for Neutrophil Migration.” 2013. Thesis, University of Illinois – Chicago. Accessed January 16, 2021. http://hdl.handle.net/10027/10374.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Liu, Xiaowen. “The ‘Go’ and ‘Stop’ Mechanisms for Neutrophil Migration.” 2013. Web. 16 Jan 2021.

Vancouver:

Liu X. The ‘Go’ and ‘Stop’ Mechanisms for Neutrophil Migration. [Internet] [Thesis]. University of Illinois – Chicago; 2013. [cited 2021 Jan 16]. Available from: http://hdl.handle.net/10027/10374.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Liu X. The ‘Go’ and ‘Stop’ Mechanisms for Neutrophil Migration. [Thesis]. University of Illinois – Chicago; 2013. Available from: http://hdl.handle.net/10027/10374

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Boston University

4. Zawawi, Khalid Hashim. Moesin mediated intracellular signalling in LPS-stimulated differentiated THP-1 cells.

Degree: Doctor of Science in Dentistry, Oral Biology, 2004, Boston University

URL: http://hdl.handle.net/2144/31303

► Lipopolysaccharide (LPS), a glycolipid found in the outer membrane of Gram negative bacteria, induces the secretion of pro-inflammatory cytokines such as tumor necrosis factor alpha… (more)

Subjects/Keywords: Gram-negative bacteria; Lipopolysaccharides; Macrophages; Moesin

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

APA (6^th Edition):

Zawawi, K. H. (2004). Moesin mediated intracellular signalling in LPS-stimulated differentiated THP-1 cells. (Doctoral Dissertation). Boston University. Retrieved from http://hdl.handle.net/2144/31303

Chicago Manual of Style (16^th Edition):

Zawawi, Khalid Hashim. “Moesin mediated intracellular signalling in LPS-stimulated differentiated THP-1 cells.” 2004. Doctoral Dissertation, Boston University. Accessed January 16, 2021. http://hdl.handle.net/2144/31303.

MLA Handbook (7^th Edition):

Zawawi, Khalid Hashim. “Moesin mediated intracellular signalling in LPS-stimulated differentiated THP-1 cells.” 2004. Web. 16 Jan 2021.

Vancouver:

Zawawi KH. Moesin mediated intracellular signalling in LPS-stimulated differentiated THP-1 cells. [Internet] [Doctoral dissertation]. Boston University; 2004. [cited 2021 Jan 16]. Available from: http://hdl.handle.net/2144/31303.

Council of Science Editors:

Zawawi KH. Moesin mediated intracellular signalling in LPS-stimulated differentiated THP-1 cells. [Doctoral Dissertation]. Boston University; 2004. Available from: http://hdl.handle.net/2144/31303

5. ZHU HONGYUAN. Cytoskeleton Regulators in the Control of Corneal Fibrosis.

Degree: 2011, National University of Singapore

URL: http://scholarbank.nus.edu.sg/handle/10635/36108

Subjects/Keywords: fibrosis; moesin; cytoskeleton; cornea; myofibroblast; keratocytes

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

APA (6^th Edition):

HONGYUAN, Z. (2011). Cytoskeleton Regulators in the Control of Corneal Fibrosis. (Thesis). National University of Singapore. Retrieved from http://scholarbank.nus.edu.sg/handle/10635/36108

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

HONGYUAN, ZHU. “Cytoskeleton Regulators in the Control of Corneal Fibrosis.” 2011. Thesis, National University of Singapore. Accessed January 16, 2021. http://scholarbank.nus.edu.sg/handle/10635/36108.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

HONGYUAN, ZHU. “Cytoskeleton Regulators in the Control of Corneal Fibrosis.” 2011. Web. 16 Jan 2021.

Vancouver:

HONGYUAN Z. Cytoskeleton Regulators in the Control of Corneal Fibrosis. [Internet] [Thesis]. National University of Singapore; 2011. [cited 2021 Jan 16]. Available from: http://scholarbank.nus.edu.sg/handle/10635/36108.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

HONGYUAN Z. Cytoskeleton Regulators in the Control of Corneal Fibrosis. [Thesis]. National University of Singapore; 2011. Available from: http://scholarbank.nus.edu.sg/handle/10635/36108

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

University of St. Andrews

6. Herron, Lissa Rocha. A study of the behaviour and interactions of the novel FERM protein Willin .

Degree: 2008, University of St. Andrews

URL: http://hdl.handle.net/10023/418

► Willin is a novel member of the Four-point-one Ezrin Radixin Moesin (FERM) protein superfamily, containing an N-terminal FERM domain most like the Ezrin-Radixin-Moesin (ERM) family… (more)

Subjects/Keywords: Willin; FERM; Merlin; Ezrin; Radixin; Moesin; Neurofascin; L1

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

APA (6^th Edition):

Herron, L. R. (2008). A study of the behaviour and interactions of the novel FERM protein Willin . (Thesis). University of St. Andrews. Retrieved from http://hdl.handle.net/10023/418

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Herron, Lissa Rocha. “A study of the behaviour and interactions of the novel FERM protein Willin .” 2008. Thesis, University of St. Andrews. Accessed January 16, 2021. http://hdl.handle.net/10023/418.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Herron, Lissa Rocha. “A study of the behaviour and interactions of the novel FERM protein Willin .” 2008. Web. 16 Jan 2021.

Vancouver:

Herron LR. A study of the behaviour and interactions of the novel FERM protein Willin . [Internet] [Thesis]. University of St. Andrews; 2008. [cited 2021 Jan 16]. Available from: http://hdl.handle.net/10023/418.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Herron LR. A study of the behaviour and interactions of the novel FERM protein Willin . [Thesis]. University of St. Andrews; 2008. Available from: http://hdl.handle.net/10023/418

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Université Paris-Sud – Paris XI

7. Rayah, Amel. Identification des voies biochimiques stimulées par le récepteur purinergique P2X7 qui sont impliquées dans le clivage protéolytique du précurseur de la protéine amyloïde (APP) : Identification of the Biochemical Pathways Stimulated by Purinergic Receptor P2X7 Involved in the Proteolytic Clivage of the Amyloid Precursor Protein (APP).

Degree: Docteur es, Aspects moléculaires et cellulaires de la biologie, 2015, Université Paris-Sud – Paris XI

URL: http://www.theses.fr/2015PA11T043

►

Le précurseur de la protéine amyloïde (APP) est une protéine transmembranaire qui, après coupure séquentielle par les sécrétases β et γ, produit des peptides Aβ… (more)

▼

Le précurseur de la protéine amyloïde (APP) est une protéine transmembranaire qui, après coupure séquentielle par les sécrétases β et γ, produit des peptides Aβ trouvés dans les plaques séniles de patientsatteints d’Alzheimer. Par contre, la forme soluble de l’APP (sAPPα), produite après coupure par une sécrétase α, augmente la survie cellulaire, la croissance des neurites et la synaptogénèse. L’APP est coupéeau site α par 3 métalloprotéases : ADAM9, ADAM10 et ADAM17.Notre laboratoire a montré que la stimulation du récepteur purinergique P2X7 (P2X7R) provoque la coupure protéolytique du précurseur de la protéine amyloïde (APP). Le Dr Delarasse a établi que la voie non amyloïdogénique est mise en jeu et que c'est le fragment sAPPα, neuroprotecteur, qui est produit. Deplus, le laboratoire a précédemment démontré que ce ne sont pas les alpha-sécrétases ADAM9, 10 et 17 qui sont responsables du clivage protéolytique de l'APP après stimulation du P2X7R dans les cellules de neuroblastome Neuro2a.Durant mes travaux de thèse, nous avons étudié la voie biochimique menant à la libération du fragments APPα. L’activation du P2X7R stimule la phosphorylation et la translocation rapide à la membrane plasmique de protéines, appelées ezrine, radixine et moesine (ERM) qui ont la capacité d’établir un lien entre la région cytosolique du P2X7R et la F-actine. Les ERM jouent un rôle crucial dans la coupure protéolytique de l’APP par les métalloprotéases ADAM. En effet, l’inhibition de l’expression des ERM par RNA interférence aboutit à une absence de coupure de l’APP. Par ailleurs, nous avons observé que les MAPKERK1/2 et JNK et la ROCKinase sont nécessaires à la phosphorylation activatrice des ERM et jouent donc un rôle en amont des ERM. Enfin, nous avons mis en évidence le rôle de la PI3K en aval des ERM.Par ailleurs, nous avons démontré que l’activation du récepteur purinergique P2X7 entraînait la coupure protéolytique de la molécule NrCAM par ADAM17 aboutissant à la libération du fragment soluble del’ectodomaine de NrCAM. Les résultats obtenus indiquent que la coupure de NrCAM est dépendante de l’activation et de la fixation des ERM à NrCAM. Ces résultats suggèrent fortement que les ERM sont indispensables à la coupure protéolytique de différents substrats après stimulation du P2X7R.Les données obtenues mettent en évidence un mécanisme moléculaire original et important qui fait jouer aux ERM un rôle central de « liens moléculaires » dans le clivage protéolytique des protéines transmembranaires. A ce stade de notre étude, nous émettons l’hypothèse que les ERM agissent en aval du récepteur P2X7, en liant les substrats et/ou les protéases qu’ils regroupent à la membrane plasmique favorisant ainsi le clivage des substrats.

The amyloid protein precursor (APP) can be cleaved in neural cells by α-secretases to produce the soluble APP ectodomain (sAPPα), which is neuroprotective. We have shown previously that activation of the purinergic receptor P2X7 (P2X7R), a member of the P2X receptor family of ATP-gated cation channels, triggers sAPPα…

Advisors/Committee Members: Kanellopoulos, Jean (thesis director).

Subjects/Keywords: APP; P2X7; Ezrine Radixine Moesine; ATP; Maladie d'Alzheimer; ERM; APP; P2X7; Ezrin Radixin Moesin; ATP; Alzheimer disease; ERM

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

APA (6^th Edition):

Rayah, A. (2015). Identification des voies biochimiques stimulées par le récepteur purinergique P2X7 qui sont impliquées dans le clivage protéolytique du précurseur de la protéine amyloïde (APP) : Identification of the Biochemical Pathways Stimulated by Purinergic Receptor P2X7 Involved in the Proteolytic Clivage of the Amyloid Precursor Protein (APP). (Doctoral Dissertation). Université Paris-Sud – Paris XI. Retrieved from http://www.theses.fr/2015PA11T043

Chicago Manual of Style (16^th Edition):

Rayah, Amel. “Identification des voies biochimiques stimulées par le récepteur purinergique P2X7 qui sont impliquées dans le clivage protéolytique du précurseur de la protéine amyloïde (APP) : Identification of the Biochemical Pathways Stimulated by Purinergic Receptor P2X7 Involved in the Proteolytic Clivage of the Amyloid Precursor Protein (APP).” 2015. Doctoral Dissertation, Université Paris-Sud – Paris XI. Accessed January 16, 2021. http://www.theses.fr/2015PA11T043.

MLA Handbook (7^th Edition):

Rayah, Amel. “Identification des voies biochimiques stimulées par le récepteur purinergique P2X7 qui sont impliquées dans le clivage protéolytique du précurseur de la protéine amyloïde (APP) : Identification of the Biochemical Pathways Stimulated by Purinergic Receptor P2X7 Involved in the Proteolytic Clivage of the Amyloid Precursor Protein (APP).” 2015. Web. 16 Jan 2021.

Vancouver:

Rayah A. Identification des voies biochimiques stimulées par le récepteur purinergique P2X7 qui sont impliquées dans le clivage protéolytique du précurseur de la protéine amyloïde (APP) : Identification of the Biochemical Pathways Stimulated by Purinergic Receptor P2X7 Involved in the Proteolytic Clivage of the Amyloid Precursor Protein (APP). [Internet] [Doctoral dissertation]. Université Paris-Sud – Paris XI; 2015. [cited 2021 Jan 16]. Available from: http://www.theses.fr/2015PA11T043.

Council of Science Editors:

Rayah A. Identification des voies biochimiques stimulées par le récepteur purinergique P2X7 qui sont impliquées dans le clivage protéolytique du précurseur de la protéine amyloïde (APP) : Identification of the Biochemical Pathways Stimulated by Purinergic Receptor P2X7 Involved in the Proteolytic Clivage of the Amyloid Precursor Protein (APP). [Doctoral Dissertation]. Université Paris-Sud – Paris XI; 2015. Available from: http://www.theses.fr/2015PA11T043

Université de Montréal

8. Panneton, Vincent. Régulation de la kinase Ste20 Slik de Drosophila par phosphorylation de la boucle d'activation.

Degree: 2015, Université de Montréal

URL: http://hdl.handle.net/1866/12107

Subjects/Keywords: Slik; Moesin; kinase; phosphorylation; épithélium; epithelium; prolifération; proliferation; drosophile; Drosophila; Biology - Molecular / Biologie - Biologie moléculaire (UMI : 0307)

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APA (6^th Edition):

Panneton, V. (2015). Régulation de la kinase Ste20 Slik de Drosophila par phosphorylation de la boucle d'activation. (Thesis). Université de Montréal. Retrieved from http://hdl.handle.net/1866/12107

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Panneton, Vincent. “Régulation de la kinase Ste20 Slik de Drosophila par phosphorylation de la boucle d'activation.” 2015. Thesis, Université de Montréal. Accessed January 16, 2021. http://hdl.handle.net/1866/12107.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Panneton, Vincent. “Régulation de la kinase Ste20 Slik de Drosophila par phosphorylation de la boucle d'activation.” 2015. Web. 16 Jan 2021.

Vancouver:

Panneton V. Régulation de la kinase Ste20 Slik de Drosophila par phosphorylation de la boucle d'activation. [Internet] [Thesis]. Université de Montréal; 2015. [cited 2021 Jan 16]. Available from: http://hdl.handle.net/1866/12107.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Panneton V. Régulation de la kinase Ste20 Slik de Drosophila par phosphorylation de la boucle d'activation. [Thesis]. Université de Montréal; 2015. Available from: http://hdl.handle.net/1866/12107

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

9. Persson, Åsa. Induction of the cytoskeletal protein radixin in the adult brain.

Degree: 2012, University of Gothenburg / Göteborgs Universitet

URL: http://hdl.handle.net/2077/30264

► Abstract Neural stem and progenitor cells (NSPCs) proliferate throughout life in two regions of the brain, namely the subventricular zone (SVZ) of the lateral ventricles… (more)

▼ Abstract Neural stem and progenitor cells (NSPCs) proliferate throughout life in two regions of the brain, namely the subventricular zone (SVZ) of the lateral ventricles and the subgranular zone of dentate gyrus in the hippocampus. In the adult SVZ, NSPCs give rise to neuroblasts that leave the SVZ for long distance migration along the rostral migratory stream (RMS), on their way to the olfactory bulb where they mature and are integrated in the neural network. Understanding how adult neuronal migration is regulated is of importance for the development of new therapeutic interventions using endogenous stem or progenitor cells for brain repair strategies. Long distance migration of neuroblasts in the RMS requires a highly dynamic cytoskeleton with the ability to respond to surrounding stimuli. In this thesis, we hypothesized that cytoskeleton rearrangement in the RMS is mediated by the ERM (Ezrin/Radixin/Moesin) family of proteins. ERM proteins regulate actin polymerization through interaction with actin and transmembrane adhesion molecules in many different parts of the body, however, limited studies exist of ERM proteins in the adult brain. In the first paper, our studies demonstrate the specific expression of radixin in neuroblasts in both the ventricular and hippocampal neurogenic niches. We also demonstrate the presence of radixin in Olig2 expressing cells throughout the adult brain. In the second study, the function of radixin was inhibited using a selective quinocarmycin analog which interrupts the ability for radixin to link the actin cytoskeleton to the membrane. Inhibition of radixin in SVZ explant cultures selectively blocked the migration of neuroblasts, whereas glial migration remained unaltered, suggesting that these populations use different ERM proteins for actin polymerization. In addition, intracerebroventricular infusion of the radixin inhibitor resulted in aberrant neuroblast chain formation and decreased neuroblast proliferation in the RMS. In the third paper, EGF infusion revealed elevated levels of radixin expression in the SVZ and RMS. EGF treatment is known to greatly reduce the migratory population in the SVZ and RMS. Accordingly, a new radixin expressing population was present in the RMS after EGF treatment and these cells also expressed Olig2. Proliferation of the radixin/Olig2+ population occurred already after 24h, even in parts of the RMS that are distal to the SVZ, suggesting local activation by EGF throughout the RMS rather than migration from the SVZ. The radixin/Olig2+ cells in the RMS were arranged in chains and migrated in explant cultures in vitro. Being negative for NG2 and CNPase, these radixin/Olig2+ cells are likely not oligodendrocyte progenitors. In the fourth study, radixin expression was induced in the peri-infarct region after cortical stroke. Unexpectedly, the number of cortical radixin/Olig2+ cells decreased after stroke and radixin was instead present in a subpopulation of activated microglia. In the healthy brain and in the contralateral cortex, microglia did not…

Subjects/Keywords: Rostral migratory stream; stroke; Neural stem cells; microglia; ezrin/radixin/moesin; Olig2

…28 The cytoskeletal proteins of the Ezrin/Radixin/Moesin family… …45 Expression of moesin and ezrin in the SVZ and RMS…

6 more images…

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APA (6^th Edition):

Persson, �. (2012). Induction of the cytoskeletal protein radixin in the adult brain. (Thesis). University of Gothenburg / Göteborgs Universitet. Retrieved from http://hdl.handle.net/2077/30264

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Chicago Manual of Style (16^th Edition):

Persson, Åsa. “Induction of the cytoskeletal protein radixin in the adult brain.” 2012. Thesis, University of Gothenburg / Göteborgs Universitet. Accessed January 16, 2021. http://hdl.handle.net/2077/30264.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

MLA Handbook (7^th Edition):

Persson, Åsa. “Induction of the cytoskeletal protein radixin in the adult brain.” 2012. Web. 16 Jan 2021.

Vancouver:

Persson �. Induction of the cytoskeletal protein radixin in the adult brain. [Internet] [Thesis]. University of Gothenburg / Göteborgs Universitet; 2012. [cited 2021 Jan 16]. Available from: http://hdl.handle.net/2077/30264.

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

Council of Science Editors:

Persson �. Induction of the cytoskeletal protein radixin in the adult brain. [Thesis]. University of Gothenburg / Göteborgs Universitet; 2012. Available from: http://hdl.handle.net/2077/30264

Note: this citation may be lacking information needed for this citation format:
Not specified: Masters Thesis or Doctoral Dissertation

10. Lubart, Quentin. Les protéines ERM , Interactions entre la membrane cellulaire et le cytosquelette : une approche biomimétique. : Interactions between ERM proteins, cell membrane and cytoskeleton : a biomimetic approach.

Degree: Docteur es, Matériaux, Mécanique, Génie civil, Electrochimie, 2016, Université Grenoble Alpes (ComUE)

URL: http://www.theses.fr/2016GREAI108

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Les protéines ERMs (Ezrine, radixine et moésine) jouent un rôle central in cellulo, dans de nombreux processus cellulaires tels que les infections, la migration et… (more)

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Les protéines ERMs (Ezrine, radixine et moésine) jouent un rôle central in cellulo, dans de nombreux processus cellulaires tels que les infections, la migration et la division cellulaire. Parmi celles-ci, la moésine est plus particulièrement impliquée dans la formation de la synapse immunologique, l’infection virale et bactérienne, et les métastases cancéreuses. D’un point de vue structural, les ERM peuvent être en conformation inactive (replies sur elles-mêmes) ou actives (ouvertes), ce qui permet leur interaction a la fois avec les constituants du cytosquelette (actine et tubuline) via leur domaine C-terminal et la membrane plasmique via leur domaine FERM. La liaison a la membrane plasmique se fait principalement et spécifiquement via un lipide de la famille des phosphoinositides, le phosphatidyl 4,5 bisphosphate (PIP2). De plus, les protéines peuvent être phosphorylées, ce qui contribue à leur ouverture structurale. Cependant, le rôle de la phosphorylation sur les interactions ERM/membrane et ERM/cytosquelette, bien que beaucoup étudié in cellulo, est peu compris au niveau moléculaire.Le but de cette thèse est précisément d’étudier, au niveau moléculaire et à l’aide de systèmes biomimétiques, les interactions entre des protéines recombinantes et des membranes biomimétiques contenant du PIP2. Pour cela, nous avons mis au point des membranes lipidiques sous forme de vésicules unilamellaires (petites ou larges) et de bicouches lipidiques supportées, qui permettent de caractériser les interactions entre protéines et membranes par des techniques biophysiques complémentaires, notamment la cosédimentation quantitative, la microscopie et spectroscopie de fluorescence, et la microbalance à cristal de quartz. Dans une première partie, nous avons étudié le rôle de la double phosphorylation de la moésine (réalisée par mutation sur site spécifique) sur les interactions moésine/membrane biomimétique, en comparaison de la protéine sauvage, les protéines recombinantes et les mutants ayant été produites et purifiées au laboratoire.Nos résultats mettent en évidence une interaction spécifique et coopérative pour le double mutant phosphomimétique alors que cette interaction est simple dans le cas de la protéine sauvage. Dans une seconde partie, nous avons employé les bicouches lipidiques supportées contenant le PIP2 pour étudier les mécanismes molécules d’adsorption de la protéine virale Gag et de ses mutants. Les méthodologies développées dans ce travail de thèse ouvrent des perspectives en biophysique moléculaires car elles sont facilement transposables à l’étude d’autres protéines sur des membranes lipidiques modèles contenant des phosphoinositides.Mots clés: Ezrine-Radixine-Moésine, phosphoinositides, PIP2, interactions protéine-lipide, membrane lipidique biomimétique, protéine virale Gag, cytosquelette.

ERM (ezrin, radixin, moesin) proteins play a central role in cellulo in a large number of physiological and pathological processes, including cell infection, migration and cell division. Among the ERMs, moesin is particularly…

Advisors/Committee Members: Picart, Catherine (thesis director), Blanchoin, Laurent (thesis director).

Subjects/Keywords: Ezrine-Radixine-Moésine; Phosphoinositides et PIP2; Cytosquelette; Membrane lipidique biomimétique; Protéine virale Gag; Interactions protéine-Lipide; Ezrin-Radixin-Moesin; Phosphoinositides and PIP2; Cytosqueleton; Biomimetic lipidic membranes; Viral Gag protein; Interaction protein-Lipid; 570

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

APA (6^th Edition):

Lubart, Q. (2016). Les protéines ERM , Interactions entre la membrane cellulaire et le cytosquelette : une approche biomimétique. : Interactions between ERM proteins, cell membrane and cytoskeleton : a biomimetic approach. (Doctoral Dissertation). Université Grenoble Alpes (ComUE). Retrieved from http://www.theses.fr/2016GREAI108

Chicago Manual of Style (16^th Edition):

Lubart, Quentin. “Les protéines ERM , Interactions entre la membrane cellulaire et le cytosquelette : une approche biomimétique. : Interactions between ERM proteins, cell membrane and cytoskeleton : a biomimetic approach.” 2016. Doctoral Dissertation, Université Grenoble Alpes (ComUE). Accessed January 16, 2021. http://www.theses.fr/2016GREAI108.

MLA Handbook (7^th Edition):

Lubart, Quentin. “Les protéines ERM , Interactions entre la membrane cellulaire et le cytosquelette : une approche biomimétique. : Interactions between ERM proteins, cell membrane and cytoskeleton : a biomimetic approach.” 2016. Web. 16 Jan 2021.

Vancouver:

Lubart Q. Les protéines ERM , Interactions entre la membrane cellulaire et le cytosquelette : une approche biomimétique. : Interactions between ERM proteins, cell membrane and cytoskeleton : a biomimetic approach. [Internet] [Doctoral dissertation]. Université Grenoble Alpes (ComUE); 2016. [cited 2021 Jan 16]. Available from: http://www.theses.fr/2016GREAI108.

Council of Science Editors:

Lubart Q. Les protéines ERM , Interactions entre la membrane cellulaire et le cytosquelette : une approche biomimétique. : Interactions between ERM proteins, cell membrane and cytoskeleton : a biomimetic approach. [Doctoral Dissertation]. Université Grenoble Alpes (ComUE); 2016. Available from: http://www.theses.fr/2016GREAI108

11. Seabrooke, Sara. Regulatory Effects of the Actin-binding Proteins Moesin and MyosinII on Synaptic Activity at the Drosophila Neuromuscular Junction.

Degree: 2010, University of Toronto

URL: http://hdl.handle.net/1807/26383

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The nervous system is made up of specialized cells which receive and respond to environmental stimuli. Intercellular communication in the nervous system is achieved predominantly… (more)

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The nervous system is made up of specialized cells which receive and respond to environmental stimuli. Intercellular communication in the nervous system is achieved predominantly through chemical synaptic transmission. Within the chemical synapse, the actin cytoskeleton plays a major role in regulating synaptic activities, although the extent and clarity in our understanding of these processes is still limited. Using the genetically pliable model, Drosophila melanogaster, this thesis begins to unravel contributions of actin binding proteins to synaptic development and physiology at the larval neuromuscular junction (NMJ). Two actin binding proteins, Moesin and Nonmuscle Myosin II (NMMII) were selected for study based on previous studies implicating them in synaptic development. Combining genetics, fluorescent imaging and electrophysiological recordings this thesis unveils previously unidentified functions for Moesin and NMMII in morphology and physiology of the Drosophila NMJ. Moesin was found to help restrain synaptic growth but did not affect synaptic physiology. By correlating morphological and electrophysiological measurements in Moesin mutants, it was determined that physiology and morphology can be independently regulated at the NMJ. NMMII was used to investigate a role for actin binding proteins in physiology at the Drosophila NMJ. By using the fluorescent imaging technique, FRAP, this becomes the first research to implicate NMMII in unstimulated synaptic vesicle mobility. FRAP indicated that vesicle mobility was highly dependent on the expression level of NMMII. Electrophysiological analysis of NMMII indicated distinct mechanisms for spontaneous and evoked vesicle release. NMMII expression exhibited a positive correlation with basal synaptic transmission and was important in mobilizing vesicles for synaptic potentiation. In addition, NMMII was found to be involved in a high frequency dependent low frequency depression. This work begins to identify how vesicles traverse within boutons and suggests differential mechanisms of synaptic release, both of which are partially dependent of NMMII expression. Studying Moesin and NMMII have revealed a complex interplay between the actin cytoskeleton and synaptic function and together this research furthers our understanding of how the actin cytoskeleton regulates synaptic activity.

PhD

Advisors/Committee Members: Stewart, Bryan, Cell and Systems Biology.

Subjects/Keywords: Drosophila; neuroscience; Moesin; Myosin; neuromuscular junction; physiology; neuron; synaptic transmission; potentiation; high frequency; N-ethylmaleimide sensitive factor; morphology; FRAP; electrophysiology; vesicle; low frequency depression; development; actin; cytoskeleton; growth; neural; nervous; 0317; 0719; 0379

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Record Details Similar Records Cite « Share

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

APA (6^th Edition):

Seabrooke, S. (2010). Regulatory Effects of the Actin-binding Proteins Moesin and MyosinII on Synaptic Activity at the Drosophila Neuromuscular Junction. (Doctoral Dissertation). University of Toronto. Retrieved from http://hdl.handle.net/1807/26383

Chicago Manual of Style (16^th Edition):

Seabrooke, Sara. “Regulatory Effects of the Actin-binding Proteins Moesin and MyosinII on Synaptic Activity at the Drosophila Neuromuscular Junction.” 2010. Doctoral Dissertation, University of Toronto. Accessed January 16, 2021. http://hdl.handle.net/1807/26383.

MLA Handbook (7^th Edition):

Seabrooke, Sara. “Regulatory Effects of the Actin-binding Proteins Moesin and MyosinII on Synaptic Activity at the Drosophila Neuromuscular Junction.” 2010. Web. 16 Jan 2021.

Vancouver:

Seabrooke S. Regulatory Effects of the Actin-binding Proteins Moesin and MyosinII on Synaptic Activity at the Drosophila Neuromuscular Junction. [Internet] [Doctoral dissertation]. University of Toronto; 2010. [cited 2021 Jan 16]. Available from: http://hdl.handle.net/1807/26383.

Council of Science Editors:

Seabrooke S. Regulatory Effects of the Actin-binding Proteins Moesin and MyosinII on Synaptic Activity at the Drosophila Neuromuscular Junction. [Doctoral Dissertation]. University of Toronto; 2010. Available from: http://hdl.handle.net/1807/26383

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Open Access Theses and Dissertations