title: Turning on ARF: the Sec7 family of guanine-nucleotide-exchange factors.
abstract: ARF proteins are important regulators of membrane dynamics and protein transport within the eukaryotic cell. The Sec7 domain is approximately 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.
authors.affiliation: Service de Biochimie et Génétique Moléculaire, CEA/Saclay, Gif-sur-Yvette, France. cathy@jonas.saclay.cea.fr
authors.forename: C L
authors.initials: CL
authors.lastname: Jackson
authors.forename: J E
authors.initials: JE
authors.lastname: Casanova
mesh_terms: D020823:ADP-Ribosylation Factor 1 / Q000378:metabolism*; D000818:Animals; D005656:Fungal Proteins / Q000737:chemistry / Q000494:pharmacology / Q000502:physiology; D020662:Guanine Nucleotide Exchange Factors / Q000737:chemistry / Q000494:pharmacology / Q000502:physiology; D006801:Humans; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae; D017386:Sequence Homology, Amino Acid
chemical_list: D005656:Fungal Proteins; D020662:Guanine Nucleotide Exchange Factors; C066755:Sec7 guanine nucleotide exchange factors; D020823:ADP-Ribosylation Factor 1