期刊
MOLECULES AND CELLS
卷 29, 期 4, 页码 311-325出版社
KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
DOI: 10.1007/s10059-010-0053-8
关键词
actin-binding protein; actin cytoskeleton; BAR protein; F-actin; filament cross-linking; filament nucleation and elongation; G-actin; Rho-GTPase; WH2
资金
- National Research Foundation (NRF) [R13-2003-009, 2009-0064846]
- NIH [GM073791]
- National Research Foundation of Korea [2008-0062303, 2009-0064846] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
The dynamic remolding of the actin cytoskeleton is a critical part of most cellular activities, and malfunction of cytoskeletal proteins results in various human diseases. The transition between two forms of actin, monomeric or G-actin and filamentous or F-actin, is tightly regulated in time and space by a large number of signaling, scaffolding and actin-binding proteins (ABPs). New ABPs are constantly being discovered in the post-genomic era. Most of these proteins are modular, integrating actin binding, protein-protein interaction, membrane-binding, and signaling domains. In response to extracellular signals, often mediated by Rho family GTPases, ABPs control different steps of actin cytoskeleton assembly, including filament nucleation, elongation, severing, capping, and depolymerization. This review summarizes structure-function relationships among ABPs in the regulation of actin cytoskeleton assembly.
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