4.7 Review

Ribosome Abundance Control Via the Ubiquitin-Proteasome System and Autophagy

Journal

JOURNAL OF MOLECULAR BIOLOGY
Volume 432, Issue 1, Pages 170-184

Publisher

ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1016/j.jmb.2019.06.001

Keywords

autophagy; ubiquitin; degradation; ribosome

Funding

  1. National Institutes of Health [R37NS083524, AG011085, RO1GM095567]

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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.

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