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- W2004818790 abstract "Regulation of synaptic membrane adenylate cyclase is likely to involve interaction between neurotransmitter receptors, G-proteins and the adenylate cyclase catalytic unit as well as several other membrane proteins and lipids. Despite intensive study of this system, regulation of guanine nucleotide binding by the G-proteins which stimulate [Gs] or inhibit [Gi] adenylate cyclase has been examined only when those proteins have been purified and removed from the influence of the membrane environment. The hydrolysis-resistant photoaffinity GTP-analog, P3-(4-azidoanilido)-P1 5'-GTP (AAGTP) is able to bind specifically to the G-proteins in rat cerebral cortex synaptic membranes and, in this study, we have used this probe to examine the specificity and selectivity of guanine nucleotide binding to each G-protein without removing those proteins from the synaptic membrane. Marked differences were noted between guanine nucleotide binding data obtained with detergent-soluble G-proteins and data from this in situ approach. In these studies it was found that the affinity of the G-proteins binding AAGTP correlated well with the expression of adenylate cyclase activity, the affinity of both forms of Gs increasing under conditions favoring the stimulation of that enzyme." @default.
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- W2004818790 date "1988-08-01" @default.
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- W2004818790 title "In situ binding of a photo-affinity GTP analog to synaptic membrane G-proteins Distribution of bound GTP analog reflects the status of adenylate cyclase" @default.
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- W2004818790 doi "https://doi.org/10.1016/0014-5793(88)81262-6" @default.
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