A study on the modulation of alpha-actinin and filamentous actin
type: CreativeWork
description: 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.
abstract: 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.
author: Kemp, James Peter
language: en
keywords: Stress fibers, Alpha-actinin
date published: 2017-08-10T19:51:51Z
date modified: 2026-07-22T22:24:34Z
provider: University of Illinois - Urbana-Champaign
publisher: Networked Digital Library of Theses and Dissertations
type: WebPage
source organization: University of Illinois at Urbana-Champaign

PropertyValue
property ID: Handle
value: http://hdl.handle.net/2142/97561