Ribosome Abundance Control Via the Ubiquitin-Proteasome System and Autophagy

被引:68
作者
An, Heeseon [1 ]
Harper, J. Wade [1 ]
机构
[1] Harvard Med Sch, Blavatnik Inst, Dept Cell Biol, 240 Longwood Ave, Boston, MA 02115 USA
基金
美国国家卫生研究院;
关键词
autophagy; ubiquitin; degradation; ribosome; QUALITY-CONTROL; ELECTRON-MICROSCOPY; RNA-POLYMERASE; KINASE COMPLEX; REVEALS; DEGRADATION; STARVATION; PROTEINS; PROTEOME; RECEPTOR;
D O I
10.1016/j.jmb.2019.06.001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Ribosomes are central to the life of a cell, as they translate the genetic code into the amino acid language of proteins. Moreover, ribosomal abundance within the cell is coordinated with protein production required for cell function or processes such as cell division. As such, it is not surprising that these elegant machines are both highly regulated at the level of both their output of newly translated proteins but also at the level of ribosomal protein expression, ribosome assembly, and ribosome turnover. In this review, we focus on mechanisms that regulate ribosome abundance through both the ubiquitin-proteasome system and forms of autophagy referred to as "ribophagy." We discussed mechanisms employed in both yeast and mammalian cells, including the various machineries that are important for recognition and degradation of ribosomal components. In addition, we discussed controversies in the field and how the development of new approaches for examining flux through the proteasomal and autophagic systems in the context of a systematic inventory of ribosomal components is necessary to fully understand how ribosome abundance is controlled under various physiological conditions. (C) 2019 Elsevier Ltd. All rights reserved.
引用
收藏
页码:170 / 184
页数:15
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