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PMID: 15118165 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Cofilin promotes actin polymerization and defines the direction of cell motility.

Science (New York, N.Y.) ·Vol. 304 ·No. 5671 ·2004-04-30 ·Pages 743-6

Ghosh M, Song X, Mouneimne G, Sidani M, Lawrence DS, Condeelis JS

Abstract

A general caging method for proteins that are regulated by phosphorylation was used to study the in vivo biochemical action of cofilin and the subsequent cellular response. By acute and local activation of a chemically engineered, light-sensitive phosphocofilin mimic, we demonstrate that cofilin polymerizes actin, generates protrusions, and determines the direction of cell migration. We propose a role for cofilin that is distinct from its role as an actin-depolymerizing factor.

MeSH Terms
Actin Depolymerizing Factors Actins/metabolism Animals Biopolymers Cell Line, Tumor Cell Movement Light Lim Kinases Microfilament Proteins/genetics,physiology Microinjections Mutation Phenylacetates/chemistry Phosphorylation Protein Binding Protein Kinases/metabolism Pseudopodia/physiology,ultrastructure RNA, Small Interfering Rats
Chemicals
Actin Depolymerizing Factors Actins Biopolymers Microfilament Proteins Phenylacetates RNA, Small Interfering alpha-bromo-alpha-(2-nitrophenyl)acetic acid Protein Kinases Lim Kinases Limk1 protein, rat
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Ghosh Mousumi
Department of Anatomy and Structural Biology, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.
Song Xiaoyan
Mouneimne Ghassan
Sidani Mazen
Lawrence David S
Condeelis John S
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
1095-9203
Published
2004-04-30
Pages
743-6
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Grants
NIGMS NIH HHS · GM38511 · United States
NIGMS NIH HHS · GM61034 · United States
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