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Originally published In Press as doi:10.1074/jbc.M207235200 on August 2, 2002

J. Biol. Chem., Vol. 277, Issue 41, 38037-38044, October 11, 2002
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Transcriptional Activity of CCAAT/Enhancer-binding Proteins Is Controlled by a Conserved Inhibitory Domain That Is a Target for Sumoylation*

Jinyong KimDagger , Carrie A. Cantwell§, Peter F. Johnson§, Curt M. PfarrDagger , and Simon C. WilliamsDagger ||

From the Dagger  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

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/EBPepsilon . Here we describe the further characterization of a C/EBPepsilon inhibitory domain termed regulatory domain I. We show that functionally related domains are present in C/EBPalpha , C/EBPbeta , and C/EBPdelta . 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/EBPepsilon regulatory domain, suggesting that sumoylation may play an important role in modulating C/EBPepsilon 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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