Dunn A Y, Melville M W, Frydman J
Department of Biological Sciences, Stanford University, Stanford, California 94305-5020, USA.
J Struct Biol. 2001 Aug;135(2):176-84. doi: 10.1006/jsbi.2001.4380.
The TCP-1 ring complex (TRiC; also called CCT, for chaperonin containing TCP-1) is a large (approximately 900 kDa) multisubunit complex that mediates protein folding in the eukaryotic cytosol. The physiological substrate spectrum of TRiC is still poorly defined. Genetic and biochemical data show that it is required for the folding of the cytoskeletal proteins actin and tubulin. Recent years have witnessed a steady stream of reports that describe other proteins that require TRiC for proper folding. Furthermore, analysis of the transit of newly synthesized proteins through TRiC in intact cells suggests that the chaperonin contributes to the folding of a distinct subset of cellular proteins. Here we review the current understanding of a role for TRiC in the folding of newly synthesized polypeptides, with a focus on some of the individual proteins that require TRiC.
TCP-1 环状复合物（TRiC；也称为CCT，即含TCP-1的伴侣蛋白）是一种大型（约900 kDa）多亚基复合物，介导真核细胞胞质溶胶中的蛋白质折叠。TRiC的生理底物谱仍不清楚。遗传和生化数据表明，它是细胞骨架蛋白肌动蛋白和微管蛋白折叠所必需的。近年来，不断有报道描述其他需要TRiC进行正确折叠的蛋白质。此外，对完整细胞中新合成蛋白质通过TRiC的转运分析表明，该伴侣蛋白有助于细胞内特定蛋白质子集的折叠。在此，我们综述了目前对TRiC在新合成多肽折叠中作用的理解，重点关注一些需要TRiC的个别蛋白质。
