Histone deacetylase 7 promotes PML sumoylation and is essential for PML nuclear body formation

Chengzhuo Gao, Chun Chen Ho, Erin Reineke, Minh Lam, Xiwen Cheng, Kristopher J. Stanya, Yu Liu, Sharmistha Chakraborty, Hsiu Ming Shih, Hung Ying Kao

Research output: Contribution to journalArticle

55 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)5658-5667
Number of pages10
JournalMolecular and Cellular Biology
Volume28
Issue number18
DOIs
StatePublished - Sep 2008

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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