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J Biol Chem, Vol. 274, Issue 43, 30495-30500, October 22, 1999
and Phosphoinositide-dependent
Protein Kinase-1 Are Required for Insulin-induced Activation of
ERK in Rat Adipocytes
,,
From the The mechanisms used by insulin to activate the
multifunctional intracellular effectors, extracellular signal-regulated
kinases 1 and 2 (ERK1/2), are only partly understood and appear to vary in different cell types. Presently, in rat adipocytes, we found that
insulin-induced activation of ERK was blocked (a) by
chemical inhibitors of both phosphatidylinositol 3-kinase (PI3K) and
protein kinase C (PKC)- J. A. Haley Veterans Hospital Research
Service, and Department of Internal Medicine, University of South
Florida College of Medicine, Tampa, Florida 33612, § Hypertension-Endocrine Branch,
, and, moreover, (b) by transient
expression of both dominant-negative 
p85 PI3K subunit and
kinase-inactive PKC-. Further, insulin effects on ERK were inhibited
by kinase-inactive 3-phosphoinositide-dependent protein
kinase-1 (PDK-1), and by mutation of Thr-410 in the activation loop of
PKC-, which is the target of PDK-1 and is essential for
PI3K/PDK-1-dependent activation of PKC-. In addition to
requirements for PI3K, PDK-1, and PKC-, we found that a tyrosine
kinase (presumably the insulin receptor), the SH2 domain of GRB2, SOS,
RAS, RAF, and MEK1 were required for insulin effects on ERK in the rat
adipocyte. Our findings therefore suggested that PDK-1 and PKC-
serve as a downstream effectors of PI3K, and act in conjunction with
GRB2, SOS, RAS, and RAF, to activate MEK and ERK during insulin action
in rat adipocytes.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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