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Journal of Biomedicine and Biotechnology
Volume 2011, Article ID 569034, 13 pages
http://dx.doi.org/10.1155/2011/569034
Review Article

Jun Dimerization Protein 2 Controls Senescence and Differentiation via Regulating Histone Modification

1Center of Excellence for Environmental Medicine, Kaohsiung Medical University, 100 Shih-Chuan 1st Road, San Ming District, Kaohsiung 80708, Taiwan
2Graduate Institute of Medicine, Kaohsiung Medical University, 100 Shih-Chuan 1st Road, San Ming District, Kaohsiung 80708, Taiwan
3Department of Molecular Cell Biology, Graduate School of Pharmaceutical Sciences, Chiba University, Chiba 260-8675, Japan
4College of Medicine, Kaohsiung Medical University Hospital, 100 Shih-Chuan 1st Road, San Ming District, Kaohsiung 80708, Taiwan
5College of Dental Medicine, Kaohsiung Medical University Hospital, 100 Shih-Chuan 1st Road, San Ming District, Kaohsiung 80708, Taiwan
6Cancer Center, Kaohsiung Medical University Hospital, 100 Shih-Chuan 1st Road, San Ming District, 807 Kaohsiung, Taiwan
7Saito Laboratory of Cell Technology, 2095-20 Yaita, Tochigi 329-1571, Japan
8Department of Molecular Preventive Medicine, Graduate School of Medicine, The University of Tokyo, Tokyo 113-0033, Japan

Received 10 June 2010; Accepted 8 September 2010

Academic Editor: Minoru Yoshida

Copyright © 2011 Yu-Chang Huang et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Abstract

Transcription factor, Jun dimerization protein 2 (JDP2), binds directly to histones and DNAs and then inhibits the p300-mediated acetylation both of core histones and of reconstituted nucleosomes that contain JDP2 recognition DNA sequences. JDP2 plays a key role as a repressor of adipocyte differentiation by regulation of the expression of the gene C/EBPδ via inhibition of histone acetylation. Moreover, JDP2-deficient mouse embryonic fibroblasts (JDP2−/− MEFs) are resistant to replicative senescence. JDP2 inhibits the recruitment of polycomb repressive complexes (PRC1 and PRC2) to the promoter of the gene encoding p16Ink4a, resulting from the inhibition of methylation of lysine 27 of histone H3 (H3K27). Therefore, it seems that chromatin-remodeling factors, including the PRC complex controlled by JDP2, may be important players in the senescence program. The novel mechanisms that underline the action of JDP2 in inducing cellular senescence and suppressing adipocyte differentiation are reviewed.