Reg1 and Snf1 regulate stress-induced relocalization of protein phosphatase-1 to cytoplasmic granules.
Glc7
Reg1
Snf1
protein phosphatase-1
stress granules
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
08 2021
08 2021
Historique:
revised:
22
02
2021
received:
02
12
2020
accepted:
03
03
2021
pubmed:
9
3
2021
medline:
8
9
2021
entrez:
8
3
2021
Statut:
ppublish
Résumé
The compartmentalization of cellular function is achieved largely through the existence of membrane-bound organelles. However, recent work suggests a novel mechanism of compartmentalization mediated by membraneless structures that have liquid droplet-like properties and arise through phase separation. Cytoplasmic stress granules (SGs) are the best characterized and are induced by various stressors including arsenite, heat shock, and glucose deprivation. Current models suggest that SGs play an important role in protein homeostasis by mediating reversible translation attenuation. Protein phosphatase-1 (PP1) is a central cellular regulator responsible for most serine/threonine dephosphorylation. Here, we show that upon arsenite stress, PP1's catalytic subunit Glc7 relocalizes to punctate cytoplasmic granules. This altered localization requires PP1's recently described maturation pathway mediated by the multifunctional ATPase Cdc48 and PP1's regulatory subunit Ypi1. Glc7 relocalization is mediated by its regulatory subunit Reg1 and its target Snf1, the AMP-dependent protein kinase. Surprisingly, Glc7 granules are highly specific to arsenite and appear distinct from canonical SGs. Arsenite induces potent translational inhibition, and translational recovery is strongly dependent on Glc7, but independent of Glc7's well-established role in regulating eIF2α. These results suggest a novel form of stress-induced cytoplasmic granule and a new mode of translational control by Glc7.
Identifiants
pubmed: 33682330
doi: 10.1111/febs.15802
pmc: PMC8373691
mid: NIHMS1708410
doi:
Substances chimiques
Saccharomyces cerevisiae Proteins
0
SNF1-related protein kinases
EC 2.7.1.-
Protein Serine-Threonine Kinases
EC 2.7.11.1
Protein Phosphatase 1
EC 3.1.3.16
REG1 protein, S cerevisiae
EC 3.1.3.16
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
4833-4848Subventions
Organisme : NIH HHS
ID : DP5 OD019800
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM135337
Pays : United States
Informations de copyright
© 2021 Federation of European Biochemical Societies.
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