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Molecular and Cellular Biology, September 2008, p. 5658-5667, Vol. 28, No. 18
0270-7306/08/$08.00+0     doi:10.1128/MCB.00874-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.

Histone Deacetylase 7 Promotes PML Sumoylation and Is Essential for PML Nuclear Body Formation{triangledown} ,{dagger}

Chengzhuo Gao,1 Chun-Chen Ho,3 Erin Reineke,1 Minh Lam,2 Xiwen Cheng,1 Kristopher J. Stanya,1 Yu Liu,1 Sharmistha Chakraborty,1,{ddagger} Hsiu-Ming Shih,3 and Hung-Ying Kao1,2*

Department of Biochemistry, School of Medicine, Case Western Reserve University, 10900 Euclid Avenue,1 Comprehensive Cancer Center of Case Western Reserve University and University Hospitals of Cleveland, Cleveland, Ohio 44106,2 Institute of Biomedical Sciences, Academia Sinica 128, Academia Road, Sec. 2, Taipei 11529, Taiwan3

Received 2 June 2008/ Accepted 2 July 2008

Promyelocytic leukemia protein (PML) sumoylation has been proposed to control the formation of PML nuclear bodies (NBs) and is crucial for PML-dependent cellular processes, including apoptosis and transcriptional regulation. However, the regulatory mechanisms of PML sumoylation and its specific roles in the formation of PML NBs remain largely unknown. Here, we show that histone deacetylase 7 (HDAC7) knockdown reduces the size and the number of the PML NBs in human umbilical vein endothelial cells (HUVECs). HDAC7 coexpression stimulates PML sumoylation independent of its HDAC activity. Furthermore, HDAC7 associates with the E2 SUMO ligase, Ubc9, and stimulates PML sumoylation in vitro, suggesting that it possesses a SUMO E3 ligase-like activity to promote PML sumoylation. Importantly, HDAC7 knockdown inhibits tumor necrosis factor alpha-induced PML sumoylation and the formation of PML NBs in HUVECs. These results demonstrate a novel function of HDAC7 and provide a regulatory mechanism of PML sumoylation.

* Corresponding author. Mailing address: Department of Biochemistry, School of Medicine, Case Western Reserve University, 10900 Euclid Ave., Cleveland, OH 44106. Phone: (216) 368-1150. Fax: (216) 368-3419. E-mail: hxk43{at}cwru.edu

{triangledown} Published ahead of print on 14 July 2008.

{dagger} Supplemental material for this article may be found at http://mcb.asm.org/.

{ddagger} Present address: Neuroscience Research Laboratory, Methodist Research Institute, E520 Noyes Building, 1800 N. Capitol Ave., Indianapolis, IN 46202.

Molecular and Cellular Biology, September 2008, p. 5658-5667, Vol. 28, No. 18
0270-7306/08/$08.00+0     doi:10.1128/MCB.00874-08
Copyright © 2008, American Society for Microbiology. All Rights Reserved.





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