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J Biol Chem, Vol. 274, Issue 36, 25308-25316, September 3, 1999
and C-
by an
Autophosphorylation-dependent Mechanism and Stimulates
Their Translocation to GLUT4 Vesicles and Other Membrane Fractions in
Rat Adipocytes
,,,,,,,
From the In rat adipocytes, insulin provoked rapid
increases in (a) endogenous immunoprecipitable combined
protein kinase C (PKC)- J. A. Haley Veterans' Hospital Research
Service and the Department of Internal Medicine, University of South
Florida College of Medicine, Tampa, Florida 33612, the ¶ Centro de
Biologia Molecular "Severo Ochoa", Universidad Autónoma,
Canto Blanco, 28049 Madrid, Spain, and the § Signal
Transduction Group, Boston Biomedical Research Institute,
Boston, Massachusetts 02114
/
activity in plasma membranes and
microsomes and (b) immunoreactive PKC- and PKC- in
GLUT4 vesicles. Activity and autophosphorylation of immunoprecipitable
epitope-tagged PKC- and PKC- were also increased by insulin
in situ and phosphatidylinositol
3,4,5-(PO4)3 (PIP3) in
vitro. Because phosphoinositide-dependent kinase-1
(PDK-1) is required for phosphorylation of activation loops of PKC-
and protein kinase B, we compared their activation. Both RO 31-8220 and
myristoylated PKC- pseudosubstrate blocked insulin-induced activation and autophosphorylation of PKC-/ but did not inhibit PDK-1-dependent (a) protein kinase B
phosphorylation/activation or (b) threonine 410 phosphorylation in the activation loop of PKC-. Also, insulin
in situ and PIP3 in vitro activated
and stimulated autophosphorylation of a PKC- mutant, in which
threonine 410 is replaced by glutamate (but not by an inactivating
alanine) and cannot be activated by PDK-1. Surprisingly, insulin
activated a truncated PKC- that lacks the regulatory (presumably
PIP3-binding) domain; this may reflect PIP3
effects on PDK-1 or transphosphorylation by endogenous full-length
PKC-. Our findings suggest that insulin activates both PKC- and
PKC- in plasma membranes, microsomes, and GLUT4 vesicles by a
mechanism requiring increases in PIP3, PDK-1-dependent phosphorylation of activation loop sites in
PKC- and , and subsequent autophosphorylation and/or transphosphorylation.
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