Molecular Structure of Cell Signalling Laboratory, The Francis Crick Institute, 1 Midland Road, London NW1 1AT, U.K.
Biochem Soc Trans. 2020 Dec 18;48(6):2615-2624. doi: 10.1042/BST20200383.
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 an 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 activity though the propensity of RING domains to dimerize differs significantly between different TRIMs and can be influenced by other regions of the protein.
TRIM 蛋白形成一个蛋白家族，其特征是具有保守的三联体基序结构域，该结构域包含一个 RING 结构域、一个或两个 B -box 结构域和一个卷曲螺旋区。这个大型蛋白家族的成员是许多细胞功能的重要调节剂，包括先天免疫反应、转录调节和细胞凋亡。其细胞功能的关键是其 E3 连接酶活性，该活性由 RING 结构域赋予。自身缔合是 TRIM 蛋白活性的一个重要特征，通过卷曲螺旋区的同源二聚化介导，在某些情况下通过三联体基序的其他结构域介导更高阶的缔合。迄今为止，在研究的许多 TRIM 家族蛋白中，RING 二聚化是 E3 连接酶酶活性的重要前提，尽管不同的 TRIM 之间 RING 结构域二聚化的倾向有很大差异，并且可以受到蛋白质的其他区域的影响。
