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Originally published In Press as doi:10.1074/jbc.M006727200 on September 29, 2000

J. Biol. Chem., Vol. 276, Issue 3, 1735-1741, January 19, 2001
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Calmodulin Kinase II Attenuation of Gene Transcription by Preventing cAMP Response Element-binding Protein (CREB) Dimerization and Binding of the CREB-binding Protein*

Xiling WuDagger § and Cynthia T. McMurrayDagger ||**

From the Dagger  Department of Molecular Pharmacology and Experimental Therapeutics, the § Mayo Graduate School, the  Department of Biochemistry and Molecular Biology, and the || Molecular Neuroscience Program, Mayo Clinic and Foundation, Rochester, Minnesota 55905

Calmodulin Kinase II (CamKII) inhibits the transcription of many CRE-dependent genes, but the mechanism of dominant transcriptional inhibition is unknown. Here we show that phosphorylation of serine 142 in CREB by CamKII leads to dissociation of the CREB dimer without impeding DNA binding capacity. CamKII-modified CREB binds to DNA efficiently as a monomer; however, monomeric CREB is unable to recruit the CREB-binding protein (CBP) even when phosphorylated at serine 133. Thus, CamKII confers a dominant inhibitory effect on transcription by preventing dimerization of CREB, and this mechanism may account for the attenuation of gene expression.

* This work was supported by the Mayo Foundation, National Institutes of Health Grants DK 43694-01A2 and MH-56207 and National Science Foundation Grant IBN 9728120 (to C. T. M.).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.

** To whom correspondence should be addressed: Dept. of Molecular Pharmacology and Experimental Therapeutics, Mayo Foundation, 200 First St., S. W., Rochester, MN 55905. Tel.: 505-284-1597; Fax: 505-284-9111; E-mail: mcmurray.cynthia@mayo.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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