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J. Biol. Chem., Vol. 277, Issue 18, 15629-15637, May 3, 2002
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From the Salt-inducible kinase (SIK), one of the
serine/threonine protein kinases, was transiently expressed in Y1 cells
during the early phase of the ACTH/cAMP-dependent protein
kinase (PKA)-mediated signal transduction. The overexpression of
SIK(N), the SIK's N-terminal kinase domain, repressed the expression
of the side chain cleavage cytochrome P450 (CYP11A) gene. To elucidate
the mechanism of the repression by SIK, several CYP11A promoter
constructs were tested for the promoter activities in the presence of
PKA and/or SIK(N). A cAMP-response element (CRE)-like sequence present
in the promoter was shown to be responsible not only for the
PKA-mediated promoter activation but also for the SIK(N)-mediated
repression. When the Gal4 DNA binding domain-linked full-length
CRE-binding protein (CREB) construct was cotransfected with Gal4
reporter gene, SIK(N) repressed the PKA-induced reporter gene
expression. However, SIK(N) could not repress the PKA-induced reporter
activity conferred by Gal4 DNA binding domain-linked basic leucine
zipper (bZIP)-less CREB or bZIP-disrupted CREB. On the other hand,
SIK(N) could repress the kinase-inducible domain-disrupted
CREB-dependent reporter gene expression in the presence of
PKA. The in vitro kinase reaction studies showed that
SIK(N) could not phosphorylate CREB, and PKA failed to phosphorylate
SIK(N). Taken together, these results suggest that SIK(N), cooperating
with PKA, may act on the CREB's bZIP domain and repress the
CREB-mediated transcriptional activation of the CYP11A gene.
Salt-inducible Kinase Represses cAMP-dependent
Protein Kinase-mediated Activation of Human Cholesterol Side Chain
Cleavage Cytochrome P450 Promoter through the CREB Basic Leucine
Zipper Domain*
§¶,¶,,,, and
Department of Molecular Physiological
Chemistry, Osaka University Medical School H-1, 2-2, Yamadaoka, Suita,
Osaka, 565-0871, Japan and the § Department of Life Science,
Kinran College, 5-25-1, Fujishirodai, Suita,
Osaka 565-0873, Japan
*
This work was supported in part by grants-in-aid for
Scientific Research from the Ministry of Education, Culture, Sports, Science and Technology and the Ministry of Health, Labor and Welfare Japan and a grant from the Uehara Memorial Foundation.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.
To whom correspondence should be addressed: Dept. of Molecular
Physiological Chemistry, Osaka University Medical School H-1, 2-2 Yamadaoka, Suita, Osaka, 565-0871, Japan. Tel.: 81-6-6879-3280; Fax:
81-6-6879-3289; E-mail: mokamoto@mr-mbio.med.osaka-u.ac.jp.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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