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Title: Proteasome storage granules protect proteasomes from autophagic degradation upon carbon starvation

Abstract

26S proteasome abundance is tightly regulated at multiple levels, including the elimination of excess or inactive particles by autophagy. In yeast, this proteaphagy occurs upon nitrogen starvation but not carbon starvation, which instead stimulates the rapid sequestration of proteasomes into cytoplasmic puncta termed proteasome storage granules (PSGs). Here, we show that PSGs help protect proteasomes from autophagic degradation. Both the core protease and regulatory particle sub-complexes are sequestered separately into PSGs via pathways dependent on the accessory proteins Blm10 and Spg5, respectively. Modulating PSG formation, either by perturbing cellular energy status or pH, or by genetically eliminating factors required for granule assembly, not only influences the rate of proteasome degradation, but also impacts cell viability upon recovery from carbon starvation. PSG formation and concomitant protection against proteaphagy also occurs in Arabidopsis, suggesting that PSGs represent an evolutionarily conserved cache of proteasomes that can be rapidly re-mobilized based on energy availability.

Authors:
ORCiD logo [1]; ORCiD logo [1]
  1. Department of Biology, Washington University in St. Louis, St. Louis, United States
Publication Date:
Sponsoring Org.:
USDOE
OSTI Identifier:
1432090
Alternate Identifier(s):
OSTI ID: 1432092
Grant/Contract Number:  
FG02-88ER13968
Resource Type:
Journal Article: Published Article
Journal Name:
eLife
Additional Journal Information:
Journal Name: eLife Journal Volume: 7; Journal ID: ISSN 2050-084X
Publisher:
eLife Sciences Publications, Ltd.
Country of Publication:
United States
Language:
English

Citation Formats

Marshall, Richard S., and Vierstra, Richard D. Proteasome storage granules protect proteasomes from autophagic degradation upon carbon starvation. United States: N. p., 2018. Web. doi:10.7554/eLife.34532.
Marshall, Richard S., & Vierstra, Richard D. Proteasome storage granules protect proteasomes from autophagic degradation upon carbon starvation. United States. doi:10.7554/eLife.34532.
Marshall, Richard S., and Vierstra, Richard D. Fri . "Proteasome storage granules protect proteasomes from autophagic degradation upon carbon starvation". United States. doi:10.7554/eLife.34532.
@article{osti_1432090,
title = {Proteasome storage granules protect proteasomes from autophagic degradation upon carbon starvation},
author = {Marshall, Richard S. and Vierstra, Richard D.},
abstractNote = {26S proteasome abundance is tightly regulated at multiple levels, including the elimination of excess or inactive particles by autophagy. In yeast, this proteaphagy occurs upon nitrogen starvation but not carbon starvation, which instead stimulates the rapid sequestration of proteasomes into cytoplasmic puncta termed proteasome storage granules (PSGs). Here, we show that PSGs help protect proteasomes from autophagic degradation. Both the core protease and regulatory particle sub-complexes are sequestered separately into PSGs via pathways dependent on the accessory proteins Blm10 and Spg5, respectively. Modulating PSG formation, either by perturbing cellular energy status or pH, or by genetically eliminating factors required for granule assembly, not only influences the rate of proteasome degradation, but also impacts cell viability upon recovery from carbon starvation. PSG formation and concomitant protection against proteaphagy also occurs in Arabidopsis, suggesting that PSGs represent an evolutionarily conserved cache of proteasomes that can be rapidly re-mobilized based on energy availability.},
doi = {10.7554/eLife.34532},
journal = {eLife},
number = ,
volume = 7,
place = {United States},
year = {Fri Apr 06 00:00:00 EDT 2018},
month = {Fri Apr 06 00:00:00 EDT 2018}
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record at 10.7554/eLife.34532

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Works referenced in this record:

Enzymatic assembly of DNA molecules up to several hundred kilobases
journal, April 2009

  • Gibson, Daniel G.; Young, Lei; Chuang, Ray-Yuan
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