Journal
CELLULAR SIGNALLING
Volume 16, Issue 4, Pages 401-413Publisher
ELSEVIER SCIENCE INC
DOI: 10.1016/j.cellsig.2003.09.012
Keywords
ADP ribosylation factor; GTPase activating proteins; enclosomes; Golgi apparatus; membrane traffic; actin; cytoskeleton; focal adhesions
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The ADP-fibosylation factor (Arf) Arf GTPase-activating proteins (GAPs) are a family of proteins that induce hydrolysis of GTP bound to Arf. A conserved domain containing a zinc finger motif mediates catalysis. The substrate, Arf GTP, affects membrane trafficking and actin remodelling. Consistent with activity as an Arf regulator, the Arf GAPs affect both of these pathways. However, the Arf GAPs are likely to have Arf-independent activities that contribute to their cellular functions. Structures of the Arf GAPs are diverse containing catalytic, protein-protein interaction and lipid interaction domains in addition to the Arf GAP domain. Some Arf GAPs have been identified and characterized on the basis of activities other than Arf GAP. Here, we describe the Arf GAP family, enzymology of some members of the Arf GAP family and known functions of the proteins. The results discussed illustrate roles for both Arf-dependent and -independent activities in the regulation of cellular architecture. (C) 2003 Elsevier Inc. All rights reserved.
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