Resveratrol and related stilbene derivatives induce stress granules with distinct clearance kinetics.

Détails

ID Serval
serval:BIB_9B39C58B180F
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Resveratrol and related stilbene derivatives induce stress granules with distinct clearance kinetics.
Périodique
Molecular biology of the cell
Auteur⸱e⸱s
Amen T., Guihur A., Zelent C., Ursache R., Wilting J., Kaganovich D.
ISSN
1939-4586 (Electronic)
ISSN-L
1059-1524
Statut éditorial
Publié
Date de publication
01/11/2021
Peer-reviewed
Oui
Volume
32
Numéro
21
Pages
ar18
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
Stress granules (SGs) are ribonucleoprotein functional condensates that form under stress conditions in all eukaryotic cells. Although their stress-survival function is far from clear, SGs have been implicated in the regulation of many vital cellular pathways. Consequently, SG dysfunction is thought to be a mechanistic point of origin for many neurodegenerative disorders, including amyotrophic lateral sclerosis (ALS). Additionally, SGs are thought to play a role in pathogenic pathways as diverse as viral infection and chemotherapy resistance. There is a growing consensus on the hypothesis that understanding the mechanistic regulation of SG physical properties is essential to understanding their function. Although the internal dynamics and condensation mechanisms of SGs have been broadly investigated, there have been fewer investigations into the timing of SG formation and clearance in live cells. Because the lifetime of SG persistence can be a key factor in their function and tendency toward pathological dysregulation, SG clearance mechanisms deserve particular attention. Here we show that resveratrol and its analogues piceatannol, pterostilbene, and 3,4,5,4'-tetramethoxystilbene induce G3BP-dependent SG formation with atypically rapid clearance kinetics. Resveratrol binds to G3BP, thereby reducing its protein-protein association valency. We suggest that altering G3BP valency is a pathway for the formation of uniquely transient SGs.
Pubmed
Open Access
Oui
Création de la notice
14/09/2021 13:11
Dernière modification de la notice
05/01/2022 7:36
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