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• W1542658963 abstract "ABSTRACT Previous results have shown that Dictyostelium discoideum mutant synag 7 is defective in the regulation of adenylate cyclase by receptor agonists in vivo and by GTPγS in vitro; the guanine nucleotide activation of adenylate cyclase is restored by the high-speed supernatant from wild-type cells. Here we report that in synag 7 membranes: (1) cyclic AMP receptors had normal levels and were regulated by guanine nucleotides as in wild-type; (2) GTP binding and high-affinity GTPase were reduced but still stimulated by cyclic AMP; (3) the supernatant from wild-type cells restored GTP binding to membranes of this mutant, and partly restored high-affinity GTPase activity; (4) the supernatant of synag 7 was ineffective in these reconstitutions and did not influence GTP binding and GTPase activities in mutant or wild-type membranes. These results suggest that the defect in mutant synag 7 is located between G-protein and adenylate cyclase, and not between receptor and G-protein. A factor in the supernatant is absent in synag 7 and appears to be essential for normal GTP binding, GTPase and activation of adenylate cyclase. This soluble heat-labile factor may represent a new molecule required for receptor-and G-protein-mediated activation of adenylate cyclase." @default.
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• W1542658963 date "1988-10-01" @default.
• W1542658963 modified "2023-10-14" @default.
• W1542658963 title "Dictyostelium discoideum mutant <i>Synag 7</i> with altered g-protein–adenylate cyclase interaction" @default.
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• W1542658963 doi "https://doi.org/10.1242/jcs.91.2.287" @default.
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