Function, evolution, and structure of J-domain proteins.
8-stranded β-sandwich domain (SBDβ)
Heat shock protein 70 (Hsp70)
J-domain proteins (JDPs)
Journal
Cell stress & chaperones
ISSN: 1466-1268
Titre abrégé: Cell Stress Chaperones
Pays: Netherlands
ID NLM: 9610925
Informations de publication
Date de publication:
01 2019
01 2019
Historique:
accepted:
06
11
2018
pubmed:
28
11
2018
medline:
19
6
2019
entrez:
28
11
2018
Statut:
ppublish
Résumé
Hsp70 chaperone systems are very versatile machines present in nearly all living organisms and in nearly all intracellular compartments. They function in many fundamental processes through their facilitation of protein (re)folding, trafficking, remodeling, disaggregation, and degradation. Hsp70 machines are regulated by co-chaperones. J-domain containing proteins (JDPs) are the largest family of Hsp70 co-chaperones and play a determining role functionally specifying and directing Hsp70 functions. Many features of JDPs are not understood; however, a number of JDP experts gathered at a recent CSSI-sponsored workshop in Gdansk (Poland) to discuss various aspects of J-domain protein function, evolution, and structure. In this report, we present the main findings and the consensus reached to help direct future developments in the field of Hsp70 research.
Identifiants
pubmed: 30478692
doi: 10.1007/s12192-018-0948-4
pii: 10.1007/s12192-018-0948-4
pmc: PMC6363617
doi:
Substances chimiques
HSP70 Heat-Shock Proteins
0
Protein Aggregates
0
Types de publication
Congress
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
7-15Subventions
Organisme : Motor Neurone Disease Association
ID : CHEETHAM/OCT15/881-792
Pays : United Kingdom
Organisme : Medical Research Council
ID : MR/N004434/1
Pays : United Kingdom
Organisme : NIGMS NIH HHS
ID : R01 GM056981
Pays : United States
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