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J Biol Chem, Vol. 273, Issue 32, 20144-20149, August 7, 1998
From the Department of Biochemistry, School of Medical Sciences,
University of Bristol, BS8 1TD, United Kingdom and
Transcription of the gene encoding the catalytic
subunit of glucose-6-phosphatase (G6Pase) is stimulated by
glucocorticoids and strongly repressed by insulin. We have explored the
signaling pathways by which insulin mediates the repression of G6Pase
transcription in H4IIE cells. Wortmannin, a phosphatidylinositide
3-kinase (PtdIns 3-kinase) inhibitor blocked the repression of G6Pase
mRNA expression by insulin. However, both rapamycin, which inhibits
p70S6 kinase activation, and PD98059, an inhibitor of mitogen-activated
protein kinase activation, were without effect. Insulin inhibited
dexamethasone-induced luciferase expression from a transiently
transfected plasmid that places the luciferase gene under the control
of the G6Pase promoter. This effect of insulin was mimicked by the
overexpression of a constitutively active PtdIns 3-kinase but not by a
constitutively active protein kinase B. Taken together, these data
demonstrate that PtdIns 3-kinase activation is both necessary and at
least partly sufficient for the repression of G6Pase expression by
insulin, but neither mitogen-activated protein kinase nor p70S6 kinase are involved. In addition, activation of protein kinase B alone is not
sufficient for repression of the G6Pase gene. These results imply the
existence of a novel signaling pathway downstream of PtdIns 3 kinase
that is involved in the regulation of G6Pase expression by insulin.
Central Role for Phosphatidylinositide 3-Kinase in the Repression
of Glucose-6-phosphatase Gene Transcription by Insulin
,, and Department of Molecular Physiology and Biophysics,
Vanderbilt University Medical School, Nashville, Tennessee 37232
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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