J-domain proteins interaction with neurodegenerative disease-related proteins.
Amyloid proteins
J-domain proteins
Molecular chaperones
Neurodegenerative diseases
Protein folding
Substrate binding
Journal
Experimental cell research
ISSN: 1090-2422
Titre abrégé: Exp Cell Res
Pays: United States
ID NLM: 0373226
Informations de publication
Date de publication:
15 02 2021
15 02 2021
Historique:
received:
28
08
2020
revised:
07
01
2021
accepted:
12
01
2021
pubmed:
19
1
2021
medline:
12
6
2021
entrez:
18
1
2021
Statut:
ppublish
Résumé
HSP70 chaperones, J-domain proteins (JDPs) and nucleotide exchange factors (NEF) form functional networks that have the ability to prevent and reverse the aggregation of proteins associated with neurodegenerative diseases. JDPs can interact with specific substrate proteins, hold them in a refolding-competent conformation and target them to specific HSP70 chaperones for remodeling. Thereby, JDPs select specific substrates and constitute an attractive target for pharmacological intervention of neurodegenerative diseases. This, under the condition that the exact mechanism of JDPs interaction with specific substrates is unveiled. In this review, we provide an overview of the structural and functional variety of JDPs that interact with neurodegenerative disease-associated proteins and we highlight those studies that identified specific residues, domains or regions of JDPs that are crucial for substrate binding.
Identifiants
pubmed: 33460589
pii: S0014-4827(21)00022-7
doi: 10.1016/j.yexcr.2021.112491
pii:
doi:
Substances chimiques
Carrier Proteins
0
HSP70 Heat-Shock Proteins
0
Molecular Chaperones
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
112491Informations de copyright
Copyright © 2021 Elsevier Inc. All rights reserved.