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J. Biol. Chem., Vol. 277, Issue 41, 38037-38044, October 11, 2002
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From the CCAAT/enhancer-binding proteins (C/EBPs) are
basic region/leucine zipper transcription factors that function as
regulators of cell growth and differentiation in numerous cell types.
We previously localized transcriptional activation and inhibitory regions in one family member, C/EBP
Transcriptional Activity of CCAAT/Enhancer-binding Proteins Is
Controlled by a Conserved Inhibitory Domain That Is a Target for
Sumoylation*
,¶, and¶
Department of Cell Biology and Biochemistry,
Texas Tech University Health Sciences Center, ¶ Southwest
Cancer Center at UMC Lubbock, Texas 79430, and § Regulation
of Cell Growth Laboratory, NCI-Frederick,
Frederick, Maryland 21702
. Here we describe the further characterization of a C/EBP inhibitory domain termed regulatory domain I. We show that functionally related domains are present in C/EBP
, C/EBP
, and C/EBP
. These domains contain an
evolutionarily conserved five-amino acid motif (the regulatory domain
motif (RDM)) that conforms to the consensus sequence
(I/V/L)KXEP. Mutagenesis studies revealed that the
residues at positions 1, 2, and 4 of the RDM are critical for
inhibitory domain function. Data base searches identified RDM-like
sequences in a number of nuclear proteins. We found that small regions
from c-Jun, JunB, and JunD containing this sequence also function as
transcriptional inhibitory domains. Importantly, the RDM is similar to
the recognition sequence for attachment of the ubiquitin-like protein,
small ubiquitin-like modifier-1 (SUMO-1), and the conserved lysine
residue of each C/EBP RDM served as an attachment site for SUMO-1.
SUMO-1 attachment decreased the inhibitory effect of the C/EBP
regulatory domain, suggesting that sumoylation may play an important
role in modulating C/EBP activity as well as that of the other C/EBP
family members.
*
This work was supported by a Scientist Development Grant
from the American Heart Association and grants from the CH Foundation, South Plains Foundation, and Houston Endowment, Inc. (to S. C. W.).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.
An Established Investigator of the American Heart Association.
To whom correspondence should be addressed. Tel.: 806-743-2524; Fax:
806-743-2990; E-mail: Simon.Williams@ttuhsc.edu.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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