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Volume 271, Number 43, Issue of October 25, 1996 pp. 27161-27166
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Protein Kinase C Alters the Responsiveness of Adenylyl Cyclases to G Protein alpha  and beta gamma Subunits

(Received for publication, May 21, 1996, and in revised form, August 1, 1996)

Gregor Zimmermann and Ronald Taussig

From the Department of Biological Chemistry, The University of Michigan Medical School, Ann Arbor, Michigan 48109-0636

The ability of protein kinase C (PKC) to regulate the responsiveness of adenylyl cyclase to different activators was assessed. Membranes prepared from Sf9 cells infected with recombinant baculoviruses encoding either type II or IV adenylyl cyclase were incubated with recombinant PKCalpha (purified from Sf9 cells), and the effects on adenylyl cyclase activity were measured after reconstitution with Gsalpha , Gbeta gamma , or forskolin. PKCalpha treatment of type II adenylyl cyclase leads to increases in basal, forskolin-stimulated, and beta gamma -stimulated activities and greater sensitivity to stimulation by Gsalpha . Paradoxically, most of the beta gamma potentiation of Gsalpha -stimulated activity is eliminated by pretreatment with PKCalpha . By contrast, treatment of type IV adenylyl cyclase with PKCalpha has little effect on the basal, forskolin-stimulated, or beta gamma -stimulated activities but markedly reduces the Gsalpha -stimulated and beta gamma -potentiated activity of this isoform. These studies demonstrate that protein kinases can alter both the activity of adenylyl cyclase isoforms and their responsiveness to G protein regulation, thereby altering the ability of adenylyl cyclases to integrate signals derived from multiple hormonal inputs.


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