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J. Biol. Chem., Vol. 277, Issue 26, 23563-23572, June 28, 2002
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From the The CCAAT/enhancer-binding proteins (C/EBPs) are
basic leucine zipper transcription factors that play important roles in
regulating cell growth and differentiation. C/EBP proteins form leucine
zipper-mediated homodimers but are also capable of heterodimerizing
with other C/EBPs in vitro. Here we show that C/EBP
Regulation of CCAAT/Enhancer-binding Protein (C/EBP) Activator
Proteins by Heterodimerization with C/EBP
(Ig/EBP)*
,,
, and**
Eukaryotic Transcriptional Regulation
Section, Regulation of Cell Growth Laboratory and the
§ Basic Research Laboratory, NCI-Frederick, Frederick,
Maryland 21702-1201 and the ¶ Department of Microbiology and
Molecular Genetics, Michigan State University,
East Lansing, Michigan 48824-1101
occurs predominantly as a heterodimer that displays rapid mobility in
gel shift assays. Biochemical fractionation and antibody supershift
assays demonstrate that the C/EBP heterodimeric partner is C/EBP
(Ig/EBP), a C/EBP protein that has been implicated as an inhibitor of
other family members. Although most cell types express
C/EBP·C/EBP heterodimers, macrophages contain a C/EBP
partner that is serologically distinct from C/EBP. We found that
C/EBP blocked the ability of C/EBP and C/EBP to activate a
reporter gene in L cell fibroblasts but did not inhibit a chimeric
C/EBP protein containing the GCN4 leucine zipper. Repression by
C/EBP occurs at the level of transactivation and requires
heterodimerization with the C/EBP partner. C/EBP was an ineffective
repressor in HepG2 hepatoma cells despite forming C/EBP heterodimers,
and C/EBP
was not effectively inhibited in either L or HepG2 cells.
Our findings demonstrate that C/EBP modulates C/EBP activity in a
cell- and isoform-specific manner.
*
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.
Supported by Grant-in-aid 9950490N from the American Heart Association.
**
To whom correspondence should be addressed: Regulation of Cell
Growth Laboratory, NCI-Frederick, Frederick, MD 21702-1201. Tel.:
301-846-1627; Fax: 301-846-5991; E-mail:
johnsopf@ncifcrf.gov.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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