SUMO E3 ligase activity of TRIM proteins

被引:157
|
作者
Chu, Y.
Yang, X. [1 ,2 ]
机构
[1] Univ Penn, Sch Med, Dept Canc Biol, 610 BRB 2-3,421 Curie Blvd, Philadelphia, PA 19096 USA
[2] Univ Penn, Sch Med, Abramson Family Canc Res Inst, Philadelphia, PA 19096 USA
关键词
TRIM proteins; SUMO E3 ligase; sumoylation; PML; Mdm2; p53; RET FINGER PROTEIN; REGULATES P53; TUMOR-SUPPRESSOR; FAMILY PROTEINS; NUCLEAR-BODIES; C-JUN; PML; UBIQUITIN; SUMOYLATION; RING;
D O I
10.1038/onc.2010.462
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
SUMOylation governs numerous cellular processes and is essential to most eukaryotic life. Despite increasing recognition of the importance of this process, an extremely limited number of small ubiquitin-like modifier (SUMO) protein ligases (E3s) have been identified. Here we show that at least some members of the functionally diverse tripartite motif (TRIM) superfamily are SUMO E3s. These TRIM proteins bind both the SUMO-conjugating enzyme Ubc9 and substrates and strongly enhance transfer of SUMOs from Ubc9 to these substrates. Among the substrates of TRIM SUMO E3s are the tumor suppressor p53 and its principal antagonist Mdm2. The E3 activity depends on the TRIM motif, suggesting it to be the first widespread SUMO E3 motif. Given the large number of TRIM proteins, our results may greatly expand the identified SUMO E3s. Furthermore, TRIM E3 activity may be an important contributor to SUMOylation specificity and the versatile functions of TRIM proteins. Oncogene (2011) 30, 1108-1116; doi:10.1038/onc.2010.462; published online 25 October 2010
引用
收藏
页码:1108 / 1116
页数:9
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