Department of Molecular Biology and Biochemistry, Simon Fraser University, Burnaby, BC, V5A 1S6, Canada.
Trends Biochem Sci. 2010 May;35(5):288-97. doi: 10.1016/j.tibs.2009.12.007. Epub 2010 Jan 28.
Actins and tubulins are abundant cytoskeletal proteins that support diverse cellular processes. Owing to the unique properties of these filament-forming proteins, an intricate cellular machinery consisting minimally of the chaperonin CCT, prefoldin, phosducin-like proteins, and tubulin cofactors has evolved to facilitate their biogenesis. More recent evidence also suggests that regulated degradation pathways exist for actin (via TRIM32) and tubulin (via parkin or cofactor E-like). Collectively, these pathways maintain the quality control of cytoskeletal proteins ('proteostasis'), ensuring the appropriate function of microfilaments and microtubules. Here, we focus on the molecular mechanisms of the quality control of actin and tubulin, and discuss emerging links between cytoskeletal proteostasis and human diseases.
肌动蛋白和微管蛋白是丰富的细胞骨架蛋白，支持多种细胞过程。由于这些纤维形成蛋白的独特性质，一种由热休克蛋白 CCT、原初折叠蛋白、磷酸二酯酶样蛋白和微管辅助蛋白组成的复杂细胞机制已经进化，以促进它们的生物发生。最近的证据还表明，肌动蛋白（通过 TRIM32）和微管蛋白（通过 parkin 或辅助因子 E 样蛋白）存在调节性降解途径。总的来说，这些途径维持着细胞骨架蛋白的质量控制（“蛋白质稳态”），确保微丝和微管的适当功能。在这里，我们专注于肌动蛋白和微管蛋白质量控制的分子机制，并讨论细胞骨架蛋白质稳态与人类疾病之间的新联系。
