Arf GAPs: multifunctional proteins that regulate membrane traffic and actin remodelling.

Abstract:

:The ADP-ribosylation 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.

journal_name

Cell Signal

journal_title

Cellular signalling

authors

Randazzo PA,Hirsch DS

doi

10.1016/j.cellsig.2003.09.012

subject

Has Abstract

pub_date

2004-04-01 00:00:00

pages

401-13

issue

4

eissn

0898-6568

issn

1873-3913

pii

S0898656803001918

journal_volume

16

pub_type

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