Regulating the 20S proteasome ubiquitin-independent degradation pathway.
Regulating the 20S proteasome ubiquitin-independent degradation pathway.
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DOI：
10.3390/biom4030862
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发表时间：
2014-09-23
期刊：
影响因子：
5.5
通讯作者：
Sharon M
中科院分区：
文献类型：
--
作者：
Ben-Nissan G;Sharon M
多年来，泛素-26S蛋白酶体降解途径被认为是蛋白酶体降解的主要途径。然而，现在越来越清楚的是，蛋白质也可以被核心 20S 蛋白酶体本身作为降解的目标。 20S 蛋白酶体的降解不需要泛素标签或 19S 调节颗粒的存在；相反，它依赖于被降解蛋白质的固有结构紊乱。因此，由于氧化、突变或老化而含有非结构化区域的蛋白质，以及自然、本质上未折叠的蛋白质，很容易受到 20S 降解的影响。与多年来获得的有关 26S 蛋白酶体降解的广泛知识不同，人们对 20S 介导的蛋白水解的控制方式知之甚少。在这里，我们描述了我们目前对协调 20S 蛋白酶体介导的降解的调节机制的理解，并强调了仍有待弥合的知识差距。
For many years, the ubiquitin-26S proteasome degradation pathway was considered the primary route for proteasomal degradation. However, it is now becoming clear that proteins can also be targeted for degradation by the core 20S proteasome itself. Degradation by the 20S proteasome does not require ubiquitin tagging or the presence of the 19S regulatory particle; rather, it relies on the inherent structural disorder of the protein being degraded. Thus, proteins that contain unstructured regions due to oxidation, mutation, or aging, as well as naturally, intrinsically unfolded proteins, are susceptible to 20S degradation. Unlike the extensive knowledge acquired over the years concerning degradation by the 26S proteasome, relatively little is known about the means by which 20S-mediated proteolysis is controlled. Here, we describe our current understanding of the regulatory mechanisms that coordinate 20S proteasome-mediated degradation, and highlight the gaps in knowledge that remain to be bridged.