Multiple functionalities of molecular chaperones revealed through systematic mapping of their interaction networks.
NAJ chaperone complex
chaperone networks
genetic interaction profiles
genetic interactions
molecular chaperone
physical interactions
protein assembly
protein–protein interaction
proteomics
proteostasis
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
08 02 2019
08 02 2019
Historique:
pubmed:
9
9
2018
medline:
27
6
2019
entrez:
9
9
2018
Statut:
ppublish
Résumé
Chaperones are a highly interactive group of proteins that function globally in many cellular processes involved in maintaining protein homeostasis. Traditional biochemical assays typically do not provide a complete view of the intricate networks through which chaperones collaborate to promote proteostasis. Recent advances in high-throughput systematic analyses of chaperone interactions have uncovered that chaperones display a remarkable cooperativity in their interactions with numerous client proteins. This cooperativity has been found to be a fundamental aspect of a properly functioning cell. Aberrant formation or improper regulation of these interactions can easily lead to disease states. Herein, we provide an overview of the use of large-scale interaction assays, whether physical (protein-protein) or genetic (epistatic), to study chaperone interaction networks. Importantly, we discuss the ongoing need for such studies to determine the mechanisms by which protein homeostasis is controlled in the cell.
Identifiants
pubmed: 30194284
pii: S0021-9258(20)36858-7
doi: 10.1074/jbc.TM118.002805
pmc: PMC6369283
doi:
Substances chimiques
Molecular Chaperones
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
2142-2150Subventions
Organisme : CIHR
ID : MOP-93778
Pays : Canada
Organisme : CIHR
ID : MOP-81256
Pays : Canada
Informations de copyright
© 2019 Rizzolo and Houry.
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