Ubiquitin recognition by the proteasome

Y. Saeki
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引用次数: 66

Abstract

The 26S proteasome is a 2.5-MDa complex responsible for the selective, ATP-dependent degradation of ubiquitylated proteins in eukaryotic cells. Substrates in hundreds cellular pathways are timely ubiquitylated and converged to the proteasome by direct recognition or by multiple shuttle factors. Engagement of substrate protein triggers conformational changes of the proteasome, which drive substrate unfolding, deubiquitylation and translocation of substrates to proteolytic sites. Recent studies have challenged the previous paradigm that Lys48-linked tetraubiquitin is a minimal degradation signal: in addition, monoubiquitylation or multiple short ubiquitylations can serve as the targeting signal for proteasomal degradation. In this review, I highlight recent advances in our understanding of the proteasome structure, the ubiquitin topology in proteasome targeting, and the cellular factors that regulate proteasomal degradation.
泛素被蛋白酶体识别
26S蛋白酶体是一种2.5-MDa复合物,负责真核细胞中泛素化蛋白的选择性,atp依赖性降解。数百种细胞通路中的底物通过直接识别或多种穿梭因子及时泛素化并聚合到蛋白酶体。底物蛋白的结合触发蛋白酶体的构象变化,从而驱动底物展开、去泛素化和底物向蛋白水解位点的易位。最近的研究挑战了先前的范式,即lys48连接的四红素是一个最小的降解信号:此外,单泛素化或多个短泛素化可以作为蛋白酶体降解的靶向信号。在这篇综述中,我重点介绍了我们对蛋白酶体结构的理解,蛋白酶体靶向中的泛素拓扑结构,以及调节蛋白酶体降解的细胞因子的最新进展。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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