A study on the modulation of alpha-actinin and filamentous actin

Cells use actin to provide structure and stability to the membrane, to drive motility, and to adhere to, pull on, and reorganize the extracellular matrix. Here I demonstrate that α-actinin-4, a well-known actin crosslinking protein and long believed to be the primary actin bundling protein for contractile actin arrays, actually inhibits bundling of actin filaments into stress fibers in epithelial cells. I show that α-actinin-4 accomplishes this by inhibiting tropomyosin dependent stabilization of filamentous actin, and maintains a dynamic basal actin array through promoting actin disassembly. Lastly I demonstrate that α-actinin-4 localization in cells can be modulated by phosphorylation of its actin-binding domain.

Name thesis:degree_name

Ph.D.

Level thesis:degree_level

Dissertation

Discipline thesis:degree_discipline

Cell and Developmental Biology

Grantor

University of Illinois at Urbana-Champaign

Year dc:date

2017

Author dc:creator

• Kemp, James Peter

Contributors dc:contributor

• Brieher, William M.
• Freeman, Brian C.
• Gillette, Martha U.
• Saif, Taher A.

• Stress fibers
• Alpha-actinin

Statement dc:rights

• Copyright 2017 James Peter Kemp Jr

Language dc:language

en

Handle dc:identifier

http://hdl.handle.net/2142/97561

OAI identifier oai:identifier

oai:www.ideals.illinois.edu:2142/97561