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Rap1GAP specifically stimulates GTP hydrolytic activity of the monomeric G protein Rap1. Physical interaction between G alpha z, a member of the Gi family of trimeric G proteins, and Rap1GAP blocks the ability of regulators of G protein signaling to stimulate GTP hydrolysis of the alpha subunit, and also attenuates the ability of activated G alpha z to inhibit adenylyl cyclase. Rap1GAP is expressed in the brain, kidney and pancreas and may act as a signal integrator to coordinate and/or integrate Gz signaling and Rap1 signaling in cells. A novel isoform of Rapl GTPase-activating protein, designated Rap1GAPII, binds specifically to G alpha z. Stimulation of the Gi-coupled M2 Muscarinic receptor translocates Rap1GAPII from the cytosol to the membrane and decreases the amount of GTP-bound Rap1, resulting in the activation of ERK/MAPK.
1300019I11Rik; 2310004O14Rik; AI427470; ARPP-90; KIAA0474; RAP1 GTPase activating protein; Rap1 GTPase-activating protein; rap1 GTPase-activating protein 1; Rap1, GTPase-activating protein 1; Rap1ga1; Rap1GAP; Rap1GAP1; RAP1GAPII; RAPGAP
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100 µg
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