Effects of SUMOylation on the subcellular localization and function of DAXX.
- Author:
Ling LI
1
;
Juan WEN
;
Qin-Hui TUO
;
Duan-Fang LIAO
Author Information
1. Institute of Pharmacy and Pharmacology, University of South China, Hengyang 421001, China.
- Publication Type:Journal Article
- MeSH:
Adaptor Proteins, Signal Transducing;
physiology;
Gene Expression Regulation;
Humans;
Nuclear Proteins;
physiology;
Sumoylation
- From:
Acta Physiologica Sinica
2013;65(1):89-95
- CountryChina
- Language:Chinese
-
Abstract:
Death domain-associated protein (DAXX) as a multifunctional nuclear protein widely resides in nucleolus, nucleoplasm, chromatin, promyelocytic leukaemia nuclear bodies (PML-NBs) and cytoplasm. It plays significant roles in transcriptional regulation, apoptosis, cell cycle and other biological activities. Small ubiquitin-like modifier (SUMO) is required for SUMOylation which is a highly conserved post-translational modification in a wide variety of cellular processes. Numerous studies demonstrated that SUMOylation has a great effect on the subcellular localization and functional regulation of DAXX. This review will provide a summary for SUMOylation of DAXX.
