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J. Biol. Chem., Vol. 277, Issue 9, 7587-7597, March 1, 2002
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From the Developmental decisions that control cell fate
are commonly regulated by the Notch signaling pathway. Activation of
transmembrane Notch receptors results in proteolytic liberation of the
intracellular domain of Notch, which translocates into the nucleus,
binds a repressor (C promoter binding factor 1/RBP-J
Repression of Activator Protein-1-mediated
Transcriptional Activation by the Notch-1 Intracellular Domain*
§,
,,**
University of Wisconsin Medical School,
Department of Pharmacology, Molecular and Cellular Pharmacology
Program, Madison, Wisconsin 53706 and ¶ University of Cincinnati
College of Medicine, Department of Molecular Genetics, Biochemistry and
Microbiology, Cincinnati, Ohio 45267-0524
, Su(H), and
Lag-1 (CSL)), and induces target genes. We found that the intracellular domain of human Notch-1 (NIC-1) represses activator protein-1 (AP-1)-mediated transactivation. Because numerous genes that control immune and inflammatory responses are AP-1-dependent and
Notch regulates immune cell function, we investigated the underlying molecular mechanisms. Repression of AP-1 by NIC-1 did not represent a
general inhibitory effect on transcription because nuclear factor B-dependent transcription and transcription driven by a
constitutive promoter and enhancer were not affected by NIC-1. The
physiological relevance of the repression was supported by the facts
that repression was apparent in multiple cell lines, endogenous AP-1
target genes were repressed, and similar concentrations of NIC-1 were
required for CSL-dependent activation and AP-1 repression.
The RBP-J-associated molecule domain of NIC-1 that mediates CSL
binding and distinct sequences necessary for transactivation were
required for repression. However, there was not a strict correlation
between the sequence requirements for CSL-dependent
activation and AP-1 repression. Repression correlated with predominant
nuclear localization of NIC-1 and was not accompanied by disruption of
c-Jun amino-terminal kinase-dependent signaling events
required for AP-1 activation or by defective AP-1 DNA binding activity.
These results provide evidence for negative cross-talk between
Notch and AP-1, which may have important consequences for controlling
diverse biological processes.
*
This work was supported by the Milwaukee Foundation, the
Leukemia Society of America, the American Heart Association-Northland Affiliate, and National Institutes of Health Grant DK50107.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.
Both authors contributed equally to this work.
**
A Leukemia Society of America Scholar and a Shaw Scientist. To whom
correspondence should be addressed: University of Wisconsin Medical
School, Dept. of Pharmacology, Molecular and Cellular Pharmacology
Program, 387 Medical Sciences Center, 1300 University Ave., Madison, WI
53706. Tel.: 608-265-6446; Fax: 608-262-1257; E-mail:
ehbresni@facstaff.wisc.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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