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Functional characterization of JMJD2A, a histone deacetylase- and retinoblastoma-binding protein.

Authors: Gray, SG  Iglesias, AH  Lizcano, F  Villanueva, R  Camelo, S  Jingu, H  Teh, BT  Koibuchi, N  Chin, WW  Kokkotou, E  Dangond, F 
Citation: Gray SG, etal., J Biol Chem. 2005 Aug 5;280(31):28507-18. Epub 2005 May 31.
Pubmed: (View Article at PubMed) PMID:15927959
DOI: Full-text: DOI:10.1074/jbc.M413687200

To effectively direct targeted repression, the class I histone deacetylases (HDACs) associate with many important regulatory proteins. In this paper we describe the molecular characterization of a member of the Jumonji domain 2 (JMJD2) family of proteins, and demonstrate its binding to both class I HDACs and the retinoblastoma protein (pRb). JMJD2 proteins are characterized by the presence of two leukemia-associated protein/plant homeodomain (LAP/PHD) zinc fingers, one JmjN, one JmjC (containing an internal retinoblastoma-binding protein 2 (RBBP2)-like sequence), and two Tudor domains. The first member of this group, JMJD2A, is widely expressed in human tissues and cell lines, and high endogenous expression of JMJD2A mRNA was found in several cell types, including human T-cell lymphotropic virus 1 (HTLV-1)-infected cell lines. JMJD2A and JMJD2B exhibit cell type-specific responses to the HDAC inhibitor trichostatin A. We show that the JMJD2A protein associates in vivo with pRb and class I HDACs, and mediates repression of E2F-regulated promoters. In HTLV-1 virus-infected cells, we find that JMJD2A binds to the viral Tax protein. Antibodies to JMJD2A recognize the native protein but also a half-sized protein fragment, the latter up-regulated in THP-1 cells during the G(2)/M phase of the cell cycle. The ability of JMJD2A to associate with pRb and HDACs and potentiate pRb-mediated repression of E2F-regulated promoters implies an important role for this protein in cell proliferation and oncogenesis.

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CRRD Object Information
CRRD ID: 9587432
Created: 2014-10-14
Species: All species
Last Modified: 2014-10-14
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.