title: Functions of cofilin in cell locomotion and invasion.
abstract: Recently, a consensus has emerged that cofilin severing activity can generate free actin filament ends that are accessible for F-actin polymerization and depolymerization without changing the rate of G-actin association and dissociation at either filament end. The structural basis of actin filament severing by cofilin is now better understood. These results have been integrated with recently discovered mechanisms for cofilin activation in migrating cells, which led to new models for cofilin function that provide insights into how cofilin regulation determines the temporal and spatial control of cell behaviour.
authors.affiliation: Department of Anatomy and Structural Biology, Albert Einstein College of Medicine of Yeshiva University, 1300 Morris Park Avenue, Bronx, New York 10461, USA. jose-javier.bravo@einstein.yu.edu
authors.forename: Jose Javier
authors.initials: JJ
authors.lastname: Bravo-Cordero
authors.forename: Marco A O
authors.initials: MA
authors.lastname: Magalhaes
authors.forename: Robert J
authors.initials: RJ
authors.lastname: Eddy
authors.forename: Louis
authors.initials: L
authors.lastname: Hodgson
authors.forename: John
authors.initials: J
authors.lastname: Condeelis
mesh_terms: D051339:Actin Depolymerizing Factors / Q000737:chemistry / Q000502:physiology*; D000199:Actins / Q000378:metabolism; D000818:Animals; D002465:Cell Movement; D022081:Cell Surface Extensions / Q000378:metabolism; D006801:Humans; D008958:Models, Molecular; D010766:Phosphorylation; D055503:Protein Multimerization; D011499:Protein Processing, Post-Translational; D017434:Protein Structure, Tertiary; D021381:Protein Transport
chemical_list: D051339:Actin Depolymerizing Factors; D000199:Actins