The role of cyclase-associated protein in regulating actin filament dynamics – more than a monomer-sequestration factor

• Type of Material: Article
• Authors: Shoichiro Ono, Emory University
• Language: English
• Date: 2013-08-01
• Publisher: Company of Biologists
• Publication Version: Final Published Version
• Copyright Statement: © 2013. Published by The Company of Biologists Ltd
• Final Published Version (URL): http://jcs.biologists.org/content/126/15/3249
• Title of Journal or Parent Work: Journal of Cell Science
• ISSN: 0021-9533
• Volume: 126
• Issue: 15
• Start Page: 3249
• End Page: 3258
• Grant/Funding Information: S.O. is supported by a grant from the National Institutes of Health (R01 AR48615). Deposited in PMC for release after 12 months.
• Keywords: Actin turnover; Cyclase-associated protein; Severing; Nucleotide exchange; ADF/cofilin
• Research Categories: Health Sciences, General; Health Sciences, Pathology; Biology, Cell

Abstract

Summary Dynamic reorganization of the actin cytoskeleton is fundamental to a number of cell biological events. A variety of actin-regulatory proteins modulate polymerization and depolymerization of actin and contribute to actin cytoskeletal reorganization. Cyclase-associated protein (CAP) is a conserved actin-monomer-binding protein that has been studied for over 20 years. Early studies have shown that CAP sequesters actin monomers; recent studies, however, have revealed more active roles of CAP in actin filament dynamics. CAP enhances the recharging of actin monomers with ATP antagonistically to ADF/cofilin, and also promotes the severing of actin filaments in cooperation with ADF/cofilin. Self-oligomerization and binding to other proteins regulate activities and localization of CAP. CAP has crucial roles in cell signaling, development, vesicle trafficking, cell migration and muscle sarcomere assembly. This Commentary discusses the recent advances in our understanding of the functions of CAP and its implications as an important regulator of actin cytoskeletal dynamics, which are involved in various cellular activities.