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.
© 2000 S. Karger AG, Basel
Received: Received: March 11, 1999
Accepted: May 3, 1999
Number of Print Pages : 8
Number of Figures : 4, Number of Tables : 0, Number of References : 28
Biological Signals and Receptors
Vol. 9, No. 1, Year 2000 (Cover Date: January-February 2000)
Journal Editor: S.F. Pang, Hong Kong; P.A. Ward, Ann Arbor, Mich.; D.P. Cardinali, Buenos Aires
ISSN: 1422–4933 (print), 1422–4992 (Online)
For additional information: http://www.karger.com/journals/bsi
Article / Publication Details
Published online: 2/23/2000
Issue release date: January–February 2000
Number of Print Pages: 8
Number of Figures: 4
Number of Tables: 0
ISSN: 1424-862X (Print)
eISSN: 1424-8638 (Online)
For additional information: http://www.karger.com/NSG
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