Crosstalk and Interplay between the Ubiquitin-Proteasome System and Autophagy.
Crosstalk and Interplay between the Ubiquitin-Proteasome System and Autophagy.
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DOI：
10.14348/molcells.2017.0115
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发表时间：
2017-07-31
影响因子：
3.8
通讯作者：
Kwon YT
中科院分区：
文献类型：
--
作者：
Ji CH;Kwon YT
真核细胞中的蛋白质水解主要由泛素（Ub）-蛋白酶体系统（UPS）和自噬溶酶体系统（以下称为自噬）介导。UPS是一种选择性的蛋白水解系统，其中底物被识别并标记有泛素，用于由蛋白酶体进行降解。自噬是利用溶酶体水解酶降解蛋白质以及各种其它细胞成分的大量降解系统。自发现之初，UPS和自噬就被认为在组分、作用机制和底物选择性方面彼此独立。最近的研究表明，细胞运行一个单一的蛋白水解网络，包括UPS和自噬，在许多方面共享显着的相似性，并在功能上相互合作，以维持蛋白稳态。在这篇综述中，我们讨论了UPS和自噬之间的串扰和相互作用的机制，强调底物选择性和细胞应激下的补偿调节。
Proteolysis in eukaryotic cells is mainly mediated by the ubiquitin (Ub)-proteasome system (UPS) and the autophagylysosome system (hereafter autophagy). The UPS is a selective proteolytic system in which substrates are recognized and tagged with ubiquitin for processive degradation by the proteasome. Autophagy is a bulk degradative system that uses lysosomal hydrolases to degrade proteins as well as various other cellular constituents. Since the inception of their discoveries, the UPS and autophagy were thought to be independent of each other in components, action mechanisms, and substrate selectivity. Recent studies suggest that cells operate a single proteolytic network comprising of the UPS and autophagy that share notable similarity in many aspects and functionally cooperate with each other to maintain proteostasis. In this review, we discuss the mechanisms underlying the crosstalk and interplay between the UPS and autophagy, with an emphasis on substrate selectivity and compensatory regulation under cellular stresses.