Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors

ARF proteins are important regulators of membrane dynamics and protein transport within the eukaryotic cell. The Sec7 domain is ∼200 amino acids in size and stimulates guanine-nucleotide exchange on members of the ARF class of small GTPases. The members of one subclass of Sec7-domain proteins are di...

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Bibliographic Details
Published in:Trends in Cell Biology 2000-02, Vol.10 (2), p.60-67
Main Authors: Jackson, Catherine L., Casanova, James E.
Format: Article
Language:English
Subjects:
ADP-Ribosylation Factor 1 - metabolism
Animals
ARF
ARF protein
brefeldin A
Brefeldin A (BFA)
Fungal Proteins - chemistry
Fungal Proteins - pharmacology
Fungal Proteins - physiology
GEF
Golgi apparatus
GTP-binding protein
GTPase
Guanine Nucleotide Exchange Factors - chemistry
Guanine Nucleotide Exchange Factors - pharmacology
Guanine Nucleotide Exchange Factors - physiology
guanine nucleotide-exchange factor
Humans
Molecular Sequence Data
PH domain
Protein Structure, Tertiary
Saccharomyces cerevisiae
Sec7 protein
Secretory pathway
Sequence Homology, Amino Acid
Trafficking
Yeast
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Summary:ARF proteins are important regulators of membrane dynamics and protein transport within the eukaryotic cell. The Sec7 domain is ∼200 amino acids in size and stimulates guanine-nucleotide exchange on members of the ARF class of small GTPases. The members of one subclass of Sec7-domain proteins are direct targets of the secretion-inhibiting drug brefeldin A, which blocks the exchange reaction by trapping a reaction intermediate in an inactive, abortive complex. A separate subclass of Sec7-domain proteins is involved in signal transduction and possess a domain that mediates membrane binding in response to extracellular signals.
ISSN:0962-8924
1879-3088
DOI:10.1016/S0962-8924(99)01699-2