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Arf GAPs as regulators of the actin cytoskeleton
Author(s) -
Randazzo Paul A.,
Inoue Hiroki,
Bharti Sanita
Publication year - 2007
Publication title -
biology of the cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.543
H-Index - 85
eISSN - 1768-322X
pISSN - 0248-4900
DOI - 10.1042/bc20070034
Subject(s) - microbiology and biotechnology , biology , cytoskeleton , actin cytoskeleton , actin , gtpase , gtpase activating protein , actin remodeling , adp ribosylation factor , effector , gtp' , g protein , signal transduction , biochemistry , cell , enzyme , endoplasmic reticulum , golgi apparatus
The Arf (ADP‐ribosylation factor) GAPs (GTPase‐activating proteins) are a family of proteins with a common catalytic domain that induces hydrolysis of GTP bound to Arf GTP‐binding proteins. At least three groups of multidomain Arf GAPs affect the actin cytoskeleton and cellular activities, such as migration and movement, that depend on the cytoskeleton. One role of the Arf GAPs is to regulate membrane remodelling that accompanies actin polymerization. Regulation of membrane remodelling is mediated in part by the regulation of Arf proteins. However, Arf GAPs also regulate actin independently of effects on membranes or Arf. These functions include acting as upstream regulators of Rho family proteins and providing a scaffold for Rho effectors and exchange factors. With multiple functional elements, the Arf GAPs could integrate signals and biochemical activities that result in co‐ordinated changes in actin and membranes necessary for a wide range of cellular functions.