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J. Biol. Chem., Vol. 280, Issue 32, 29117-29127, August 12, 2005

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Identification of the Ankyrin Repeat Proteins ANKRA and RFXANK as Novel Partners of Class IIa Histone Deacetylases^*

Audrey H. Wang, Serge Grégoire, Eleni Zika¶, Lin Xiao, Cathy S. Li, Hongwei Li, Kenneth L. Wright||, Jenny P. Ting¶, and Xiang-Jiao Yang**

From the Molecular Oncology Group, Department of Medicine, McGill University Health Centre, Montreal, Quebec H3A 1A1, Canada, ^¶Lineberger Comprehensive Cancer Center and Department of Microbiology and Immunology, The University of North Carolina at Chapel Hill, Chapel Hill, North Carolina 27599, and ^||H. Lee Moffitt Cancer Center and Research Institute, University of South Florida, Tampa, Florida 33612

Eighteen human histone deacetylases (HDACs) have been identified, and according to their sequence similarity to yeast homologs, these enzymes are grouped into distinct classes. Within class II, HDAC4, HDAC5, HDAC7, and HDAC9 share similar domain organization both within the N-terminal extension and the C-terminal catalytic domain, thus forming a subclass known as class IIa. These HDACs function as signal-responsive transcriptional corepressors. To gain further insight into their function and regulation, we utilized an N-terminal fragment of HDAC4 as bait in yeast two-hybrid screens, which uncovered myocyte enhancer factor 2C, 14-3-3, and ankyrin repeat family A protein (ANKRA). ANKRA is a poorly characterized protein with an ankyrin repeat domain similar to RFXANK, a subunit of the trimeric transcription factor RFX. Mutations on genes of the RFX subunits and the coactivator CIITA are responsible for the bare lymphocyte syndrome, an immunodeficiency disorder attributed to the lack of major histocompatibility complex class II (MHCII) antigens. Through its ankyrin repeat domain, RFXANK interacted with HDAC4. Two RFXANK-binding sites were found on HDAC4 with one located within residues 118–279 and another within residues 448–666. Interestingly, this deacetylase also interacted with CIITA. Consistent with the physical interaction with RFXANK and CIITA, HDAC4 and homologs repressed MHCII expression. These results identify ANKRA, RFXANK, and CIITA as novel targets of class IIa HDACs and suggest that these deacetylases play a role in regulating MHCII expression.

Received for publication, January 10, 2005 , and in revised form, June 9, 2005.

^* This work was supported by funds from the Canadian Cancer Society through the National Cancer Institute of Canada and from the Canada Foundation for Innovation. 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.

Both authors contributed equally to this work.

^** To whom correspondence should be addressed: McGill University Health Centre-RVH, Rm. H5.41, 687 Pine Ave. West, Montreal, Quebec H3A 1A1, Canada. Tel.: 514-934-1934 (ext. 34490); Fax: 514-843-1478; E-mail: xiang-jiao.yang{at}mcgill.ca.

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