Advanced search options

Advanced Search Options 🞨

Browse by author name (“Author name starts with…”).

Find ETDs with:

in
/  
in
/  
in
/  
in

Written in Published in Earliest date Latest date

Sorted by

Results per page:

You searched for +publisher:"University of North Carolina" +contributor:("Thompson, Peter"). One record found.

Search Limiters

Last 2 Years | English Only

No search limiters apply to these results.

▼ Search Limiters


University of North Carolina

1. Thompson, Peter. The structural and functional consequences of the interaction of the vinculin tail domain with F-actin and PIP2.

Degree: Biochemistry and Biophysics, 2015, University of North Carolina

Vinculin is an essential, highly-conserved eukaryotic scaffolding protein. It localizes to focal adhesions and adherens juctions, where it assists in physically linking the actin cytoskeleton to the adhesive structure. Loss of vinculin causes embryonic lethality with observable cardiovascular and neural defects. Vinculin is comprised of three domains: a large helical head domain, an unstructured proline-rich linker, and a helical tail. Vinculin functions as a scaffold, alternating between an autoinhibited conformation in which it cannot bind ligands, and an open conformation in which it is free to bind ligands at all three domains. The tail domain binds a variety of ligands, two of which are F-actin and phosphatidylinositol 4,5-bisphosphate (PIP2). Both interactions lack good structural models, which has hindered the development of tools to understand the specific biological functions these interactions play. Using a variety of biochemical and biophysical techniques and tools, we have developed new structural models for these interactions. The PIP2 model shows how the basic residues in helices 1 and 2 specifically recognize PIP2, while basic residues on helix 3 are responsible for membrane association. Actin-binding, conversely, is driven by a hydrophobic patch on helix 4. The application of cryo-electron microscopy has also revealed some of the conformational changes that take place in the tail domain when it binds F-actin: helix 4 straightens and helix 1 is discharged from the helix bundle. Additionally, we characterize the backbone dynamics of Vt by nuclear magnetic resonance. These experiments reveal the presence of μs-ms motions that reside where the C-terminal arm interacts with the helix bundle. These motions may be involved in the conformational change that takes place upon actin binding. Advisors/Committee Members: Thompson, Peter, Campbell, Sharon, Errede, Beverly, Collins, Edward, Cox, Adrienne, Lee, Andrew.

Subjects/Keywords: Biophysics; Biochemistry; School of Medicine; Department of Biochemistry and Biophysics

Record DetailsSimilar RecordsGoogle PlusoneFacebookTwitterCiteULikeMendeleyreddit

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

APA (6th Edition):

Thompson, P. (2015). The structural and functional consequences of the interaction of the vinculin tail domain with F-actin and PIP2. (Thesis). University of North Carolina. Retrieved from https://cdr.lib.unc.edu/record/uuid:f8dcee81-c727-40cc-94ad-8d3a7736d4a1

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):

Thompson, Peter. “The structural and functional consequences of the interaction of the vinculin tail domain with F-actin and PIP2.” 2015. Thesis, University of North Carolina. Accessed January 26, 2021. https://cdr.lib.unc.edu/record/uuid:f8dcee81-c727-40cc-94ad-8d3a7736d4a1.

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

MLA Handbook (7th Edition):

Thompson, Peter. “The structural and functional consequences of the interaction of the vinculin tail domain with F-actin and PIP2.” 2015. Web. 26 Jan 2021.

Vancouver:

Thompson P. The structural and functional consequences of the interaction of the vinculin tail domain with F-actin and PIP2. [Internet] [Thesis]. University of North Carolina; 2015. [cited 2021 Jan 26]. Available from: https://cdr.lib.unc.edu/record/uuid:f8dcee81-c727-40cc-94ad-8d3a7736d4a1.

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

Council of Science Editors:

Thompson P. The structural and functional consequences of the interaction of the vinculin tail domain with F-actin and PIP2. [Thesis]. University of North Carolina; 2015. Available from: https://cdr.lib.unc.edu/record/uuid:f8dcee81-c727-40cc-94ad-8d3a7736d4a1

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

.