Journal
AUTOPHAGY
Volume 14, Issue 11, Pages 2029-2031Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/15548627.2018.1515531
Keywords
ATP; Blm10; carbon starvation; pH; proteaphagy; proteasome; proteasome storage granules; Spg5; ubiquitin; Ubp3
Categories
Funding
- U.S. Department of Energy Office of Science
- Office of Basic Energy Science
- Chemical Sciences, Geosciences and Biosciences Division [DE-FG02-88ER13968]
- National Science Foundation
- Plant Genome Research Program [IOS-1329956]
- National Institutes of Health
- National Institute of General Medical Science [R01-GM124452-01A1]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM124452] Funding Source: NIH RePORTER
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Autophagic degradation of proteasomes (termed proteaphagy) is a conserved mechanism by which cells eliminate excess or damaged particles. This clearance is induced rapidly when organisms are starved for nitrogen and, because proteasomes are highly abundant, their breakdown likely makes an important contribution to the amino acid pools necessary for survival. By contrast, our recent studies found that proteasomes are not degraded in response to carbon starvation, even though bulk macroautophagy is similarly activated. Instead, carbon starvation induces sequestration of proteasomes into membrane-less cytoplasmic condensates previously termed proteasome storage granules (PSGs), which protect proteasomes from autophagic degradation. Preserving proteasomes in PSGs enhances the ability of yeast cells to recover from a variety of stresses, implying that rapid remobilization of stored proteasomes when conditions improve is advantageous to cell fitness. Consequently, the choice of whether to save or degrade proteasomes can profoundly impact cell survival.
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