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J. Biol. Chem., Vol. 281, Issue 43, 32272-32283, October 27, 2006

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CTIP2 Associates with the NuRD Complex on the Promoter of p57KIP2, a Newly Identified CTIP2 Target Gene^*

Acharawan Topark-Ngarm¹, Olga Golonzhka¹, Valerie J. Peterson, Brian Barrett, Jr., Brigetta Martinez², Kristi Crofoot, Theresa M. Filtz, and Mark Leid^¶3

From the Departments of Pharmaceutical Sciences, Biochemistry and Biophysics, and ^¶Environmental Health Sciences Center, Oregon State University, Corvallis, Oregon 97331

Chicken ovalbumin upstream promoter transcription factor (COUP-TF)-interacting protein 2 (CTIP2), also known as Bcl11b, is a transcriptional repressor that functions by direct, sequence-specific DNA binding activity or by recruitment to the promoter template by interaction with COUP-TF family members. CTIP2 is essential for both T cell development and axonal projections of corticospinal motor neurons in the central nervous system. However, little is known regarding the molecular mechanism(s) by which CTIP2 contributes to either process. CTIP2 complexes that were isolated from SK-N-MC neuroblastoma cells were found to harbor substantial histone deacetylase activity, which was likely conferred by the nucleosome remodeling and deacetylation (NuRD) complex. CTIP2 was found to associate with the NuRD complex through direct interaction with both RbAp46 and RbAp48, and components of the NuRD complex were found to be recruited to an artificial promoter template in a CTIP2-dependent manner in transfected cells. Finally, the NuRD complex and CTIP2 were found to co-occupy the promoter template of p57KIP2, a gene encoding a cyclin-dependent kinase inhibitor, and identified herein as a novel transcriptional target of CTIP2 in SK-N-MC cells. Therefore, it seems likely that the NuRD complex may be involved in transcriptional repression of CTIP2 target genes and contribute to the function(s) of CTIP2 within a neuronal context.

Received for publication, March 24, 2006 , and in revised form, August 7, 2006.

^* These studies were supported by Grant GM60852 from the National Institutes of Health (to M. L.) and by an NIEHS Center Grant ES00210 to the Oregon State University Environmental Health Sciences Center. 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.

¹ Both authors contributed equally to this work.

² Supported by Summer Fellowship T35 ES07316 from NIEHS, National Institutes of Health.

³ To whom correspondence should be addressed: Dept. of Pharmaceutical Sciences, College of Pharmacy, Oregon State University, Corvallis, OR 97331. Tel.: 541-737-5809; Fax: 541-737-3999; E-mail: Mark.Leid{at}oregonstate.edu.

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