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J. Biol. Chem., Vol. 277, Issue 41, 38863-38869, October 11, 2002
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From the It is reported that
3-phosphoinositide-dependent protein kinase-1 (PDK-1) is
activated in a phosphatidylinositol
3,4,5-trisphosphate-dependent manner and phosphorylates
Akt, p70S6 kinase, and atypical protein kinase C (PKC), but its
function on insulin signaling is still unclear. We cloned a full-length
pdk-1 cDNA from a human brain cDNA library, and the
adenovirus to overexpress wild type PDK-1 (PDK-1WT) or
membrane-targeted PDK-1 (PDK-1CAAX) was constructed. Overexpressed
PDK-1WT existed mainly at cytosol, and PDK-1CAAX was located at the
plasma membrane. In 3T3-L1 adipocytes, insulin induced mobility shift
of PDK-1 protein, but overexpressed PDK-1WT and CAAX were shifted at
the basal state. Insulin stimulated tyrosine phosphorylation of
PDK-1WT, but PDK-1CAAX was already tyrosine-phosphorylated at the basal
state. Overexpression of PDK-1WT led to a full activation of PKC The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF017995.
Membrane Localization of 3-Phosphoinositide-dependent
Protein Kinase-1 Stimulates Activities of Akt and Atypical Protein
Kinase C but Does Not Stimulate Glucose Transport and Glycogen
Synthesis in 3T3-L1 Adipocytes*
,§,,,,,,,, and
Third Department of Medicine and
¶ Department of Anatomy, Shiga University of Medical Science,
Seta, Otsu, Shiga 520-2192, Japan
/
without insulin stimulation but showed only the minimum effects to
stimulate phosphorylation of Akt and GSK-3. In contrast, the
overexpression of PDK-1CAAX caused phosphorylation of Akt and GSK-3
more strongly without insulin stimulation. However, PDK-1CAAX did not
affect 2-deoxyglucose uptake and inhibited glycogen synthesis,
surprisingly. Finally, PDK-1CAAX expression inhibited insulin-induced
ERK1/2 phosphorylation in a dose-dependent manner. Taken
together, the translocation of PDK-1 from cytosol to the plasma
membrane is critical for Akt and GSK-3 activation. On the other hand,
only atypical PKC and Akt activation was insufficient for stimulation
of glucose transport, and constitutive activation of Akt-GSK-3 pathway
may inhibit glycogen synthesis and MAPK cascade in 3T3-L1 adipocytes.
*
This work was supported in part by a grant-in-aid from the
Ministry of Education, Science, Sports and Culture, Japan (to H. M.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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