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J. Biol. Chem., Vol. 276, Issue 11, 8516-8523, March 16, 2001
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From the CAAT/enhancer-binding proteins
(C/EBPs) play an important role in the regulation of gene expression in
insulin-responsive tissues. We have found that a complex containing
C/EBP
Insulin Suppresses Transactivation by CAAT/Enhancer-binding
Proteins
(C/EBP)
SIGNALING TO p300/CREB-BINDING PROTEIN BY PROTEIN KINASE B
DISRUPTS INTERACTION WITH THE MAJOR ACTIVATION DOMAIN OF
C/EBP
*
§,,,
,
University of Illinois at Chicago College of
Medicine and Veterans Affairs Chicago Health Care System, Chicago,
Illinois 60612, the ¶ Research Genetics, Huntsville, Alabama
35801, and the ** Eukaryotic Transcriptional Regulation Section,
Regulation of Cell Growth Laboratory, NCI, Frederick Cancer Research
and Development Center, Frederick, Maryland 20892-0822
interacts with an insulin response sequence in the
insulin-like growth factor-binding protein-1 (IGFBP-1) gene and
that a C/EBP-binding site can mediate effects of insulin on promoter
activity. Here, we examined mechanisms mediating this effect of
insulin. The ability of insulin to suppress promoter activity via a
C/EBP-binding site is blocked by LY294002, a phosphatidylinositol
3-kinase inhibitor, but not by rapamycin, which blocks
activation of p70S6 kinase. Dominant negative
phosphatidylinositol 3-kinase and protein kinase B (PKB) block the
effect of insulin, while activated PKB suppresses promoter function via
a C/EBP-binding site, mimicking the effect of insulin. Coexpression
studies indicate that insulin and PKB suppress transactivation by
C/EBP, but not C/EBP
, and that N-terminal transactivation domains
in C/EBP are required. Studies with Gal4 fusion proteins reveal that
insulin and PKB suppress transactivation by the major activation domain
in C/EBP (AD II), located between amino acids 31 and 83. Studies
with E1A protein indicate that interaction with p300/CBP is required
for transactivation by AD II and the effect of insulin and PKB. Based on a consensus sequence, we identified a PKB phosphorylation site (Ser1834) within the region of p300/CBP known to
bind C/EBP. Mammalian two-hybrid studies indicate that insulin and
PKB disrupt interactions between this region of p300 and AD II and that
Ser1834 is critical for this effect. Signaling by PKB and
phosphorylation of Ser1834 may play an important role in
modulating interactions between p300/CBP and transcription factors and
mediate effects of insulin and related growth factors on gene expression.
*
This work was supported in part by National Institutes of
Health, NIDDK, Grant DK41430 and the Department of Veterans Affairs Merit Review Program.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.
Present address: Section of Rheumatology (M/C 733), Dept. of
Medicine, University of Illinois at Chicago, 900 South Ashland Ave.,
Chicago, IL 60607.
To whom all correspondence should be addressed: Rm. 5A122A
Research (MP 151), Veterans Affairs Chicago Health Care System (West
Side), 820 South Damen Ave., Chicago, IL 60612. Tel.:
312-666-6500 (ext. 57427); Fax: 312-455-5877; E-mail:
unterman@uic.edu.
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