Affiliation:
1. Department of Cell and Molecular Biology, St. Jude Children’s Research Hospital, Memphis, TN, USA.
2. Howard Hughes Medical Institute, St. Jude Children’s Research Hospital, Memphis, TN, USA.
Abstract
Tailoring stress responses
When faced with environmental stress, cells respond by shutting down cellular processes such as translation and nucleocytoplasmic transport. At the same time, cells preserve cytoplasmic messenger RNAs in structures known as stress granules, and many cellular proteins are modified by the covalent addition of ubiquitin, which has long been presumed to reflect degradation of stress-damaged proteins (see the Perspective by Dormann). Maxwell
et al.
show that cells generate distinct patterns of ubiquitination in response to different stressors. Rather than reflecting the degradation of stress-damaged proteins, this ubiquitination primes cells to dismantle stress granules and reinitiate normal cellular activities once the stress is removed. Gwon
et al.
show that persistent stress granules are degraded by autophagy, whereas short-lived granules undergo a process of disassembly that is autophagy independent. The mechanism of this disassembly depends on the initiating stress.
Science
, abc3593 and abf6548, this issue p.
eabc3593
and p.
eabf6548
; see also abj2400, p.
1393
Funder
National Institutes of Health
Howard Hughes Medical Institute
Amyotrophic Lateral Sclerosis Association
Publisher
American Association for the Advancement of Science (AAAS)
Cited by
137 articles.
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