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J Biol Chem, Vol. 274, Issue 13, 8589-8596, March 26, 1999
From the Protein kinase B (PKB), also known as Akt or
RAC-PK, is a serine/threonine kinase that can be activated by growth
factors via phosphatidylinositol 3-kinase. In this article we show that PKC
Protein Kinase C
Is a Negative Regulator of Protein Kinase B
Activity
,,, and
Institute of Biomembranes, Department of
Molecular Cell Biology, Utrecht University, 3584 CH Utrecht, The
Netherlands and ¶ The Netherlands Cancer Institute, Department of
Cellular Biochemistry, 1066 CX Amsterdam, The Netherlands
but not PKC
and PKC
can co-immunoprecipitate PKB from CHO cell lysates. Association of PKB with PKC was also found in COS-1 cells transiently expressing PKB and PKC, and moreover we found that
this association is mediated by the AH domain of PKB. Stimulation of
COS-1 cells with platelet-derived growth factor (PDGF) resulted in a
decrease in the PKB-PKC interaction. The use of kinase-inactive mutants of both kinases revealed that dissociation of the complex depends upon PKB activity. Analysis of the activities of the
interacting kinases showed that PDGF-induced activation of PKC was
not affected by co-expression of PKB. However, both PDGF- and
p110-CAAX-induced activation of PKB were significantly abolished in
cells co-expressing PKC. In contrast, co-expression of a kinase-dead
PKC mutant showed an increased induction of PKB activity upon PDGF
treatment. Downstream signaling of PKB, such as the inhibition of
glycogen synthase kinase-3, was also reduced by co-expression of
PKC. A clear inhibitory effect of PKC was found on the
constitutively active double PKB mutant (T308D/S473D). In summary, our
results demonstrate that PKB interacts with PKC in vivo
and that PKC acts as a negative regulator of PKB.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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