Mechanisms of Small Heat Shock Proteins.
Journal
Cold Spring Harbor perspectives in biology
ISSN: 1943-0264
Titre abrégé: Cold Spring Harb Perspect Biol
Pays: United States
ID NLM: 101513680
Informations de publication
Date de publication:
01 10 2019
01 10 2019
Historique:
pubmed:
6
3
2019
medline:
21
10
2020
entrez:
6
3
2019
Statut:
epublish
Résumé
Small heat shock proteins (sHSPs) are ATP-independent chaperones that delay formation of harmful protein aggregates. sHSPs' role in protein homeostasis has been appreciated for decades, but their mechanisms of action remain poorly understood. This gap in understanding is largely a consequence of sHSP properties that make them recalcitrant to detailed study. Multiple stress-associated conditions including pH acidosis, oxidation, and unusual availability of metal ions, as well as reversible stress-induced phosphorylation can modulate sHSP chaperone activity. Investigations of sHSPs reveal that sHSPs can engage in transient or long-lived interactions with client proteins depending on solution conditions and sHSP or client identity. Recent advances in the field highlight both the diversity of function within the sHSP family and the exquisite sensitivity of individual sHSPs to cellular and experimental conditions. Here, we will present and highlight current understanding, recent progress, and future challenges.
Identifiants
pubmed: 30833458
pii: cshperspect.a034025
doi: 10.1101/cshperspect.a034025
pmc: PMC6771367
pii:
doi:
Substances chimiques
Heat-Shock Proteins, Small
0
Metals
0
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NEI NIH HHS
ID : R01 EY017370
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM008268
Pays : United States
Informations de copyright
Copyright © 2019 Cold Spring Harbor Laboratory Press; all rights reserved.
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