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Nat Rev Mol Cell Biol. 2011 Jun;12(6):362-75. doi: 10.1038/nrm3117. Epub 2011 May 18.

ARF family G proteins and their regulators: roles in membrane transport, development and disease.

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1
Laboratory of Cell Biology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892, USA. jdonalds@helix.nih.gov

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  • Nat Rev Mol Cell Biol. 2011;12(8):533.

Abstract

Members of the ADP-ribosylation factor (ARF) family of guanine-nucleotide-binding (G) proteins, including the ARF-like (ARL) proteins and SAR1, regulate membrane traffic and organelle structure by recruiting cargo-sorting coat proteins, modulating membrane lipid composition, and interacting with regulators of other G proteins. New roles of ARF and ARL proteins are emerging, including novel functions at the Golgi complex and in cilia formation. Their function is under tight spatial control, which is mediated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs) that catalyse GTP exchange and hydrolysis, respectively. Important advances are being gained in our understanding of the functional networks that are formed not only by the GEFs and GAPs themselves but also by the inactive forms of the ARF proteins.

PMID:
21587297
PMCID:
PMC3245550
DOI:
10.1038/nrm3117
[Indexed for MEDLINE]
Free PMC Article
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