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Originally published as MBC in Press, 10.1091/mbc.E07-11-1203 on May 7, 2008

Vol. 19, Issue 7, 3020-3027, July 2008

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Signal-dependent Regulation of Transcription by Histone Deacetylase 7 Involves Recruitment to Promyelocytic Leukemia Protein Nuclear Bodies

Chengzhuo Gao*,{dagger}, Xiwen Cheng*,{dagger}, Minh Lam{dagger}, Yu Liu*,{dagger}, Qing Liu*,{dagger}, Kun-Sang Chang{ddagger}, and Hung-Ying Kao*,{dagger}

*Department of Biochemistry, School of Medicine, Case Western Reserve University, Cleveland, OH 44106; {dagger}The Comprehensive Cancer Center of Case Western Reserve University and University Hospitals of Cleveland, Cleveland, OH 44106; and {ddagger}Department of Molecular Pathology, University of Texas M.D. Anderson Cancer Center, Houston, TX 77030

Submitted December 1, 2007; Revised March 24, 2008; Accepted April 30, 2008
Monitoring Editor: A. Gregory Matera

Promyelocytic leukemia protein (PML) nuclear bodies (NBs) are dynamic subnuclear compartments that play roles in several cellular processes, including apoptosis, transcriptional regulation, and DNA repair. Histone deacetylase (HDAC) 7 is a potent corepressor that inhibits transcription by myocyte enhancer factor 2 (MEF2) transcription factors. We show here that endogenous HDAC7 and PML interact and partially colocalize in PML NBs. Tumor necrosis factor (TNF)-{alpha} treatment recruits HDAC7 to PML NBs and enhances association of HDAC7 with PML in human umbilical vein endothelial cells. Consequently, TNF-{alpha} promotes dissociation of HDAC7 from MEF2 transcription factors and the promoters of MEF2 target genes such as matrix metalloproteinase (MMP)-10, leading to accumulation of MMP-10 mRNA. Conversely, knockdown of PML enhances the association between HDAC7 and MEF2 and decreases MMP-10 mRNA accumulation. Accordingly, ectopic expression of PML recruits HDAC7 to PML NBs and leads to activation of MEF2 reporter activity. Notably, small interfering RNA knockdown of PML decreases basal and TNF-{alpha}-induced MMP-10 mRNA accumulation. Our results reveal a novel mechanism by which PML sequesters HDAC7 to relieve repression and up-regulate gene expression.

This was published online ahead of print in MBC in Press (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E07-11-1203) on May 7, 2008.

Address correspondence to: Hung-Ying Kao (hxk43{at}cwru.edu)




This article has been cited by other articles:


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C. Gao, C.-C. Ho, E. Reineke, M. Lam, X. Cheng, K. J. Stanya, Y. Liu, S. Chakraborty, H.-M. Shih, and H.-Y. Kao
Histone Deacetylase 7 Promotes PML Sumoylation and Is Essential for PML Nuclear Body Formation
Mol. Cell. Biol., September 15, 2008; 28(18): 5658 - 5667.
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