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You searched for +publisher:"University of North Carolina" +contributor:("Schaller, Michael D."). Showing records 1 – 3 of 3 total matches.

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University of North Carolina

1. Alan, Jamie. TYROSINE KINASE MODULATION OF TRAFFICKING AND BIOLOGICAL FUNCTIONS OF THE ATYPICAL RHO GTPASE, WRCH-1.

Degree: Pharmacology, 2010, University of North Carolina

Wrch-1 is an atypical Rho family small GTPase with roles in oncogenic transformation, epithelial cell morphogenesis, osteoclastogenesis, and migration. We have shown previously that Wrch-1 membrane localization and biological functions are modulated by reversible addition of a palmitate at its C-terminal membrane targeting domain. Most GTPases have at least two membrane targeting signals but no additional signals for Wrch-1 were known. We now show that the subcellular localization of Wrch-1 is responsive to growth factors contained in serum and is modulated by Src-mediated tyrosine phosphorylation. Upon stimulation with serum, Wrch-1 became phosphorylated on the evolutionarily conserved residue Y254 in its C-terminal membrane-targeting region, and relocalized from plasma membrane (PM) to endosomal compartments. Wrch-1 is known to interact with the adapter proteins Grb2 and Nck that in turn interact with growth factor receptor tyrosine kinases. We therefore next evaluated Wrch-1 modulation by RTK ligands such as EGF or PDGF. Wrch-1 was tyrosine phosphorylated in response to EGF treatment in time- and dose-dependent manner, and this was blocked by pretreatment with pharmacological inhibitors of either Src or EGFR. Wrch-1 relocalized rapidly from PM to endosomes upon EGF stimulation, similar to serum stimulation. Wrch-1 was phosphorylated at Y254 downstream of constitutively active forms of EGFR and HER2, including the deletion mutant EGFRvIII. Functionally, the phosphodeficient Wrch-1 mutant Y254F was enhanced in Wrch-1-mediated migration, cystogenesis and transformation. Thus, EGFR, Src dependent, C-terminal tyrosine phosphorylation of Wrch-1 may represent a novel feedback mechanism to down-regulate its activity. Consistent with this hypothesis, Wrch-1-GTP and effector activation are decreased after serum stimulated tyrosine phosphorylation and subsequent endosomal relocalization. Also, we observed that phosphodeficient Wrch-1 remained GTP-bound and plasma membrane-localized in the presence or absence or serum, whereas a phosphomimetic mutant remained GDP-bound and localized at endosomes. Thus, EGFR-mediated, Src-dependent C-terminal tyrosine phosphorylation of Wrch-1 may be a negative feedback mechanism to regulate both the trafficking and biological activities of Wrch-1. C-terminal tyrosine phosphorylation represents a new paradigm in posttranslational control of small GTPase localization and biological function. Advisors/Committee Members: Alan, Jamie, Cox, Adrienne, Der, Channing, Schaller, Michael D., Johnson, Gary, Rogers, Stephen.

Subjects/Keywords: School of Medicine; Department of Pharmacology

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

APA (6th Edition):

Alan, J. (2010). TYROSINE KINASE MODULATION OF TRAFFICKING AND BIOLOGICAL FUNCTIONS OF THE ATYPICAL RHO GTPASE, WRCH-1. (Thesis). University of North Carolina. Retrieved from https://cdr.lib.unc.edu/record/uuid:afbc9ce5-f21d-4707-8744-357971e1eb3b

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

Chicago Manual of Style (16th Edition):

Alan, Jamie. “TYROSINE KINASE MODULATION OF TRAFFICKING AND BIOLOGICAL FUNCTIONS OF THE ATYPICAL RHO GTPASE, WRCH-1.” 2010. Thesis, University of North Carolina. Accessed October 26, 2020. https://cdr.lib.unc.edu/record/uuid:afbc9ce5-f21d-4707-8744-357971e1eb3b.

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

MLA Handbook (7th Edition):

Alan, Jamie. “TYROSINE KINASE MODULATION OF TRAFFICKING AND BIOLOGICAL FUNCTIONS OF THE ATYPICAL RHO GTPASE, WRCH-1.” 2010. Web. 26 Oct 2020.

Vancouver:

Alan J. TYROSINE KINASE MODULATION OF TRAFFICKING AND BIOLOGICAL FUNCTIONS OF THE ATYPICAL RHO GTPASE, WRCH-1. [Internet] [Thesis]. University of North Carolina; 2010. [cited 2020 Oct 26]. Available from: https://cdr.lib.unc.edu/record/uuid:afbc9ce5-f21d-4707-8744-357971e1eb3b.

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

Council of Science Editors:

Alan J. TYROSINE KINASE MODULATION OF TRAFFICKING AND BIOLOGICAL FUNCTIONS OF THE ATYPICAL RHO GTPASE, WRCH-1. [Thesis]. University of North Carolina; 2010. Available from: https://cdr.lib.unc.edu/record/uuid:afbc9ce5-f21d-4707-8744-357971e1eb3b

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


University of North Carolina

2. Cai, Xinming. Cytoskeletal Signaling Proteins: Complex Regulatory Mechanisms and Roles in Innate Immunity.

Degree: Cell Biology and Physiology, 2007, University of North Carolina

In animals, most of the tissues are surrendered by extracellular matrix. The extracellular matrix plays multiple roles in maintaining the function of organs. It not only provides physical support to assemble the cells into an intact tissue but also sends signals to surrounding cells to regulate several cellular behaviors, such as proliferation and anti-apoptosis. The major contact between extracellular matrix and cells is mediated by focal adhesions, a transmembrane protein complex working as a hub to convert the matrix/cell interaction into a chemical signaling. Just like a canonical signaling pathway, focal adhesion signaling cascade is composed of receptors, enzymes and scaffolding proteins. The interplay of these elements precisely transmits the extracellular signal into cells to induce downstream effects. The work described here represents a collection of studies to decipher the detail mechanism of adhesion signaling. The activation of FAK is an essential event in adhesion signal transduction. In chapter II, FRET technology was applied to visualize the spatial and temporal activation of FAK in living cells. PIP2 was identified as a FAK binding partner. That also promotes the activation of FAK via conformational change. In addition to the FAK regulation mechanism, a novel paxillin modification was identified in chapter III. Phosphorylation of paxillin on serine 126 and 130, which is mediated by an ERK/GSK-3 dual kinase mechanism, regulates the cytoskeleton reorganization. Adhesion signaling is critical for multiple biological events, such as angiogenesis, neurite extension, and inflammation. Innate immunity works as the first barrier to fight against microbe infection. It not only directly destroys pathogens but also activates the antigen specific adaptive immune system. The roles of adhesion signaling proteins in innate immunity were also investigated in chapter II and III. The paxillin is phosphorylated by ERK and GSK-3 following LPS stimulation in macrophages, which is required for LPS induced macrophage spreading. In Fcγ receptor meditated phagocytosis, Pyk2 is activated and accumulated to phagocytotic cup during phagocytosis. The deletion or inactivation of Pyk2 impairs phagocytosis in macrophage. The work presented here expands our understanding of how focal adhesion proteins regulate multiple singling pathways. Advisors/Committee Members: Cai, Xinming, Schaller, Michael D..

Subjects/Keywords: School of Medicine; Department of Cell Biology and Physiology

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

APA (6th Edition):

Cai, X. (2007). Cytoskeletal Signaling Proteins: Complex Regulatory Mechanisms and Roles in Innate Immunity. (Thesis). University of North Carolina. Retrieved from https://cdr.lib.unc.edu/record/uuid:57c9a2dc-a7a5-4706-a319-e2e03204241d

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

Chicago Manual of Style (16th Edition):

Cai, Xinming. “Cytoskeletal Signaling Proteins: Complex Regulatory Mechanisms and Roles in Innate Immunity.” 2007. Thesis, University of North Carolina. Accessed October 26, 2020. https://cdr.lib.unc.edu/record/uuid:57c9a2dc-a7a5-4706-a319-e2e03204241d.

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

MLA Handbook (7th Edition):

Cai, Xinming. “Cytoskeletal Signaling Proteins: Complex Regulatory Mechanisms and Roles in Innate Immunity.” 2007. Web. 26 Oct 2020.

Vancouver:

Cai X. Cytoskeletal Signaling Proteins: Complex Regulatory Mechanisms and Roles in Innate Immunity. [Internet] [Thesis]. University of North Carolina; 2007. [cited 2020 Oct 26]. Available from: https://cdr.lib.unc.edu/record/uuid:57c9a2dc-a7a5-4706-a319-e2e03204241d.

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

Council of Science Editors:

Cai X. Cytoskeletal Signaling Proteins: Complex Regulatory Mechanisms and Roles in Innate Immunity. [Thesis]. University of North Carolina; 2007. Available from: https://cdr.lib.unc.edu/record/uuid:57c9a2dc-a7a5-4706-a319-e2e03204241d

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


University of North Carolina

3. Scheswohl, Danielle Marie. Interactions that contribute to FAK activation.

Degree: Cell Biology and Physiology, 2006, University of North Carolina

Focal adhesion kinase (FAK) is an important regulatory protein that integrates signals from integrins and growth factor receptors to control cell growth, survival, and migration. FAK function is tightly regulated and the complete mechanism of activation remains to be resolved. The FAT domain of FAK associates with the scaffolding protein paxillin as a major mechanism of FAK localization. Structural insights have been used to design point mutations to disrupt FAK binding to paxillin and resulting defects in FAK function have been characterized. The FERM domain of FAK is thought to play an important role in relaying biological signals. This domain is involved in an intramolecular interaction with the FAK catalytic domain that severely inhibits activity. I hypothesize that FERM domain associations disrupt the inhibitory association between the FERM and catalytic domains, thus activating FAK. A mutagenesis strategy has been used to identify binding sites on the FERM domain. Advisors/Committee Members: Scheswohl, Danielle Marie, Schaller, Michael D., University of North Carolina at Chapel Hill.

Subjects/Keywords: School of Medicine; Department of Cell Biology and Physiology

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

APA (6th Edition):

Scheswohl, D. M. (2006). Interactions that contribute to FAK activation. (Thesis). University of North Carolina. Retrieved from https://cdr.lib.unc.edu/record/uuid:ef7a3cea-448c-41ca-a3e0-92793d4a301c

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

Chicago Manual of Style (16th Edition):

Scheswohl, Danielle Marie. “Interactions that contribute to FAK activation.” 2006. Thesis, University of North Carolina. Accessed October 26, 2020. https://cdr.lib.unc.edu/record/uuid:ef7a3cea-448c-41ca-a3e0-92793d4a301c.

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

MLA Handbook (7th Edition):

Scheswohl, Danielle Marie. “Interactions that contribute to FAK activation.” 2006. Web. 26 Oct 2020.

Vancouver:

Scheswohl DM. Interactions that contribute to FAK activation. [Internet] [Thesis]. University of North Carolina; 2006. [cited 2020 Oct 26]. Available from: https://cdr.lib.unc.edu/record/uuid:ef7a3cea-448c-41ca-a3e0-92793d4a301c.

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

Council of Science Editors:

Scheswohl DM. Interactions that contribute to FAK activation. [Thesis]. University of North Carolina; 2006. Available from: https://cdr.lib.unc.edu/record/uuid:ef7a3cea-448c-41ca-a3e0-92793d4a301c

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

.