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Originally published In Press as doi:10.1074/jbc.M305680200 on June 16, 2003

J. Biol. Chem., Vol. 278, Issue 35, 33416-33421, August 29, 2003
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Modification of CCAAT/Enhancer-binding Protein-{beta} by the Small Ubiquitin-like Modifier (SUMO) Family Members, SUMO-2 and SUMO-3*

Erin M. Eaton and Linda Sealy {ddagger}

From the Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, Tennessee 37232

CCAAT/enhancer-binding protein-{beta} (C/EBP{beta}) activator isoforms, C/EBP{beta}-1 and C/EBP{beta}-2, differ by only 23 amino acids in the human; however, evidence is accumulating that these transcription factors are functionally distinct. Here we demonstrate that C/EBP{beta}-1, but not C/EBP{beta}-2, is conjugated to the small ubiquitin-like modifier (SUMO) family members, SUMO-2 and SUMO-3 despite the fact that the SUMO target consensus is present in both isoforms of this transcription factor. This conjugation is dependent on the integrity of the extreme N terminus of C/EBP{beta}-1 and requires lysine 173 in the human protein. Furthermore, mutation of this lysine relieves the repression of the cyclin D1 promoter by C/EBP{beta}-1 without altering the subnuclear localization of C/EBP{beta}-1. The sumoylation of C/EBP{beta}-1 is likely to be important in the functional differences observed between C/EBP{beta}-1 and C/EBP{beta}-2.

Received for publication, May 30, 2003

* The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

{ddagger} To whom correspondence should be addressed. Tel.: 615-322-3224; Fax: 615-322-7236; E-mail: linda.sealy{at}mcmail.vanderbilt.edu.


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