Putting it all together： intrinsic and extrinsic mechanisms governing proteasome biogenesis
Putting it all together： intrinsic and extrinsic mechanisms governing proteasome biogenesis作者机构：Department of Biomedical Sciences Florida State University College of Medicine Tallahassee FL 32306 USA Department of Biology Indiana University-Purdue Universi~ Indianapolis Indianapolis IN 46202 USA
出 版 物：《Frontiers in Biology》 (生物学前沿（英文版）)
年 卷 期：2017年第12卷第1期
页 面：19-48页
核心收录：
学科分类：0710[理学-生物学] 0831[工学-生物医学工程（可授工学、理学、医学学位）] 0830[工学-环境科学与工程（可授工学、理学、农学学位）] 07[理学] 1001[医学-基础医学(可授医学、理学学位)] 0836[工学-生物工程] 0713[理学-生态学]
基 金：supported in part by start-up funds from the Florida State University College of Medicine (R. J.T.Jr.) by a Research Support Funds Grant from Indiana University- Purdue University Indianapolis (A.R.K.)
主 题：proteasome assembly assembly chaperones ubiquitin-proteasome system proteolysis macromolecular complex
摘 要：BACKGROUND： The 26S proteasome is at the heart of the ubiquitin-proteasome system, which is the key cellular pathway for the regulated degradation of proteins and enforcement of protein quality control. The 26S proteasome is an unusually large and complicated protease comprising a 28-subunit core particle （CP） capped by one or two 19-subunit regulatory particles （RP）. Multiple activities within the RP process incoming ubiquitinated substrates for eventual degradation by the barrel-shaped CE The large size and elaborate architecture of the proteasome have made it an exceptional model for understanding mechanistic themes in macromolecular assembly. OBJECTIVE： In the present work, we highlight the most recent mechanistic insights into proteasome assembly, with particular emphasis on intrinsic and extrinsic factors regulating proteasome biogenesis. We also describe new and exciting questions arising about how proteasome assembly is regulated and deregulated in normal and diseased cells. METHODS： A comprehensive literature search using the PubMed search engine was performed, and key findings yielding mechanistic insight into proteasome assembly were included in this review. RESULTS： Key recent studies have revealed that proteasome biogenesis is dependent upon intrinsic features of the subunits themselves as well as extrinsic factors, many of which function as dedicated chaperones. CONCLUSION： Cells rely on a diverse set of mechanistic strategies to ensure the rapid, efficient, and faithful assembly of proteasomes from their cognate subunits. Importantly, physiological as well as pathological changes to proteasome assembly are emerging as exciting paradigms to alter protein degradation in vivo.
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