Ubiquitination is essential for recovery of cellular activities after heat shock

Eukaryotic cells respond to stress through adaptive programs that include reversible shutdown of key cellular processes, the formation of stress granules, and a global increase in ubiquitination. The primary function of this ubiquitination is thought to be for tagging damaged or misfolded proteins f...

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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2021-06, Vol.372 (6549), p.eabc3593-eabc3593
Main Authors: Maxwell, Brian A, Gwon, Youngdae, Mishra, Ashutosh, Peng, Junmin, Nakamura, Haruko, Zhang, Ke, Kim, Hong Joo, Taylor, J Paul
Format: Article
Language:English
Subjects:
Active Transport, Cell Nucleus
Animals
Arsenite
Autophagy
Cell Line
Cells, Cultured
Cellular stress response
Cellular structure
Community Resources
Constituents
Cytoplasmic Granules - metabolism
Degradation
Dismantling
Environmental stress
Feedback (Response)
Granular materials
Granule cells
Heat shock
Heat stress
Heat tolerance
Heat-Shock Response
Humans
Kidneys
Mammalian cells
Mammals
Mice
Neurons
Osmotic Pressure
Oxidative Stress
Phagocytosis
Pluripotency
Proteasomes
Protein Biosynthesis
Protein folding
Proteins
Proteolysis
Proteome - metabolism
Proteomes
Proteomics
Ribonucleoproteins - metabolism
Shutdowns
Stem cells
Stress, Physiological
Transcriptomes
Translation
Ubiquitin
Ubiquitinated Proteins - metabolism
Ubiquitination
Ultraviolet Rays
Valosin Containing Protein - antagonists & inhibitors
Valosin Containing Protein - metabolism
Valosin-containing protein
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Summary:Eukaryotic cells respond to stress through adaptive programs that include reversible shutdown of key cellular processes, the formation of stress granules, and a global increase in ubiquitination. The primary function of this ubiquitination is thought to be for tagging damaged or misfolded proteins for degradation. Here, working in mammalian cultured cells, we found that different stresses elicited distinct ubiquitination patterns. For heat stress, ubiquitination targeted specific proteins associated with cellular activities that are down-regulated during stress, including nucleocytoplasmic transport and translation, as well as stress granule constituents. Ubiquitination was not required for the shutdown of these processes or for stress granule formation but was essential for the resumption of cellular activities and for stress granule disassembly. Thus, stress-induced ubiquitination primes the cell for recovery after heat stress.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.abc3593