Three serine-to-alanine mutants of the α subunit of the heterotrimeric G protein Gz (αz) were examined for their signaling properties in the presence of phorbol ester treatment. All three αz mutants resembled wild-type αz in their abilities to inhibit αs-stimulated type 6 adenylyl cyclase (AC6) and phorbol ester treatment reduced their magnitudes of inhibition. Depending on the permissive condition, the βγ-mediated stimulation of type 2 adenylyl cyclase (AC2) was differentially regulated by αz and the three mutants. Mutation of Ser27 but not Ser16 of αz affected the efficient release of βγ subunits upon receptor activation and abolished the stimulation of phosphorylated but not αs-stimulated AC2.
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