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PMID: 12892779 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S. Review

Arf and its many interactors.

Current opinion in cell biology ·Vol. 15 ·No. 4 ·2003-08-00 ·Pages 396-404

Nie Z, Hirsch DS, Randazzo PA

Abstract

Arf GTP-binding proteins regulate membrane traffic and actin remodeling. Similar to other GTP-binding proteins, a complex of Arf-GTP with an effector protein mediates Arf function. Arf interacts with at least three qualitatively different types of effectors. First, it interacts with structural proteins, the vesicle coat proteins. The second type of effector is lipid-metabolizing enzymes, and the third comprises those proteins that bind to Arf-GTP but whose biochemical or biological functions are not yet clearly defined. Arf interacts with two other families of proteins, the exchange factors and the GTPase-activating proteins. Recent work examining the functional relationships among the diverse Arf interactors has led to reconsideration of the prevailing paradigms for Arf action.

MeSH Terms
ADP-Ribosylation Factor 1/metabolism ADP-Ribosylation Factors/metabolism Amino Acid Sequence Animals Coated Vesicles/metabolism GTPase-Activating Proteins/metabolism Humans Intracellular Membranes/metabolism Lipid Metabolism Transport Vesicles/metabolism
Chemicals
ARFGAP1 protein, human ARFGAP3 protein, human GTPase-Activating Proteins ADP-Ribosylation Factor 1 ADP-Ribosylation Factors
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Nie Zhongzhen
Laboratory of Cellular Oncology, Center for Cancer Research, National Cancer Institute, Building 37, Room 4118, Bethesda, MD 20892, USA.
Hirsch Dianne S
Randazzo Paul A
Article Info
Journal
Current opinion in cell biology
Abbr.
Curr Opin Cell Biol
ISSN
0955-0674
Published
2003-08-00
Pages
396-404
Language
English
Region
England
NLM ID
8913428
Subset
IM
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