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The shape of the ARF molecule is dependent upon the form to which it is bound, allowing it to serve in a regulatory capacity. ARF requires assistance from other proteins in order to switch between binding to GTP and GDP. GTPase activating proteins.
This entry describes a family of small GTPase activating proteins, for example ARF1-directed GTPase-activating protein, the cycle control GTPase activating protein (GAP) GCS1 which is important for the regulation of the ADP ribosylation factor ARF, a member of the Ras superfamily of GTP-binding proteins [PMID: 9446556]. The GTP-bound form of ARF is essential for the maintenance of normal Golgi morphology, it participates in recruitment of coat proteins which are required for budding and fission of membranes.
In their active, guanosine triphosphatebound (GTP-bound) state ARFs associate with membranes and trigger the recruitment of cytosolic proteins to the membrane. The switch to the GTPbound tate is under the control of a family of ARF-directed guanine-nucleotideexchange proteins containing a Sec7-homology domain (for review see ref. 1). The subsequent deactivation of ARFs and their dissociation from membranes depends on the hydrolysis of bound GTP. However, ARF proteins are devoid of intrinsic GTPase activity, and GTP hydrolysis depends on the action of GTPase-activating proteins.
[Show abstract] [Hide abstract] ABSTRACT: Arf1 is a GTP binding protein that functions at a number of cellular sites to control membrane traffic and actin remodeling. Arf1 is regulated by site-specific GTPase-activating proteins (GAPs). The combined results of crystallographic and biochemical studies have led to the proposal that Arf1 GAPs differ in the specific interface formed with Arf1. To test this hypothesis, we have used mutagenesis to examine the interaction of three Arf GAPs (ASAP1, AGAP1, and ArfGAP1) with switch 1, switch 2, and alpha helix3 of Arf1.
Submitted name: GTP-ase activating protein for ArfImported
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GTPase-activating protein for the ADP ribosylation factor family. May serve as a scaffold to bring together molecules to form signaling modules controlling vesicle trafficking, adhesion and cytoskeletal organization. Increases the speed of cell migration, as well as the size and rate of formation of protrusions, possibly by targeting PAK1 to adhesions and the leading edge of lamellipodia. Sequesters inactive non-tyrosine-phosphorylated paxillin in cytoplasmic complexes.