Does it take two to tango? RING domain self-association and activity in TRIM E3 ubiquitin ligases

被引:39
|
作者
Fiorentini, Filippo [1 ]
Esposito, Diego [1 ]
Rittinger, Katrin [1 ]
机构
[1] Francis Crick Inst, Mol Struct Cell Signalling Lab, 1 Midland Rd, London NW1 1AT, England
基金
英国医学研究理事会; 英国惠康基金;
关键词
CATALYTIC ACTIVATION; STRUCTURAL INSIGHTS; PROTEIN; TRIM5-ALPHA; FAMILY; MECHANISM; IMMUNITY; ENZYMES; BINDING; ROLES;
D O I
10.1042/BST20200383
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
TRIM proteins form a protein family that is characterized by a conserved tripartite motif domain comprising a RING domain, one or two B-box domains and a coiled-coil region. Members of this large protein family are important regulators of numerous cellular functions including innate immune responses, transcriptional regulation and apoptosis. Key to their cellular role is their E3 ligase activity which is conferred by the RING domain. Self-association is art important characteristic of TRIM protein activity and is mediated by homodimerization via the coiled-coil region, and in some cases higher order association via additional domains of the tripartite motif. In many of the TRIM family proteins studied thus far, RING dimerization is an important prerequisite for E3 ligase enzymatic activi though the propensity of RING domains to dimerize differs significantly between different TRIMs and can be influenced by other regions of the protein.
引用
收藏
页码:2615 / 2624
页数:10
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