2. Academic Validation
  3. Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors

Role of SUMO-interacting motif in Daxx SUMO modification, subnuclear localization, and repression of sumoylated transcription factors

  • Mol Cell. 2006 Nov 3;24(3):341-54. doi: 10.1016/j.molcel.2006.10.019.
Ding-Yen Lin 1,  Yen-Sung Huang,  Jen-Chong Jeng,  Hong-Yi Kuo,  Che-Chang Chang,  Ting-Ting Chao,  Chun-Chen Ho,  Yun-Ching Chen,  Tong-Ping Lin,  Hsin-I Fang,  Chih-Chang Hung,  Ching-Shu Suen,  Ming-Jing Hwang,  Kun-Sang Chang,  Gerd G Maul,  Hsiu-Ming Shih
Affiliations

Affiliation

  • 1 Institute of Biomedical Sciences, Academia Sinica, Taipei 11529, Taiwan, Republic of China.
PMID: 17081986 DOI: 10.1016/j.molcel.2006.10.019
Abstract

Small ubiquitin-like modifier (SUMO) modification has emerged as an important posttranslational control of protein functions. Daxx, a transcriptional corepressor, was reported to repress the transcriptional potential of several transcription factors and target to PML oncogenic domains (PODs) via SUMO-dependent interactions. The mechanism by which Daxx binds to sumoylated factors mediating transcriptional and subnuclear compartmental regulation remains unclear. Here, we define a SUMO-interacting motif (SIM) within Daxx and show it to be crucial for targeting Daxx to PODs and for transrepression of several sumoylated transcription factors, including Glucocorticoid Receptor (GR). In addition, the capability of Daxx SIM to bind SUMO also controls Daxx sumoylation. We further demonstrate that arsenic trioxide-induced sumoylation of PML correlates with a change of endogenous Daxx partitioning from GR-regulated gene promoter to PODs and a relief of Daxx repression on GR target gene expression. Our results provide mechanistic insights into Daxx in SUMO-dependent transcriptional control and subnuclear compartmentalization.

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