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J Biol Chem, Vol. 274, Issue 49, 34859-34867, December 3, 1999
From the Cell Signaling Laboratory, New England Biolabs,
Beverly, Massachusetts 01915
Although activation of protein kinase C (PKC) is
known to promote cell survival and protect against cell death, the PKC
targets and pathways that serve this function have remained elusive.
Here we demonstrate that two potent activators of PKC,
12-O-tetradecanoylphorbol-13-acetate and bryostatin, both
stimulate phosphorylation of Bad at Ser112, a site known to
regulate apoptotic cell death by interleukin-3. PKC inhibitors but not
PI 3-kinase/Akt inhibitors block
12-O-tetradecanoylphorbol-13-acetate-stimulated Bad
phosphorylation. PKC isoforms tested in vitro were unable to phosphorylate Bad at Ser112, suggesting that PKC acts
indirectly to activate a downstream Bad kinase. p90RSK and
family members RSK-2 and RSK-3 are activated by phorbol ester and
phosphorylate Bad at Ser112 both in vitro and
in vivo. p90RSK stimulates binding of Bad to
14-3-3 and blocks Bad-mediated cell death in a
Ser112-dependent manner. These findings suggest
that p90RSK can function in a PKC-dependent
pathway to promote cell survival via phosphorylation and inactivation
of Bad-mediated cell death.
p90RSK Blocks Bad-mediated Cell Death via a Protein
Kinase C-dependent Pathway
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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