Identification of a HTT-specific binding motif in DNAJB1 essential for suppression and disaggregation of HTT.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
10 08 2022
10 08 2022
Historique:
received:
05
01
2022
accepted:
26
07
2022
entrez:
10
8
2022
pubmed:
11
8
2022
medline:
13
8
2022
Statut:
epublish
Résumé
Huntington's disease is a neurodegenerative disease caused by an expanded polyQ stretch within Huntingtin (HTT) that renders the protein aggregation-prone, ultimately resulting in the formation of amyloid fibrils. A trimeric chaperone complex composed of Hsc70, DNAJB1 and Apg2 can suppress and reverse the aggregation of HTTExon1Q
Identifiants
pubmed: 35948542
doi: 10.1038/s41467-022-32370-5
pii: 10.1038/s41467-022-32370-5
pmc: PMC9365803
doi:
Substances chimiques
Amyloid
0
DNAJB1 protein, human
0
HSP40 Heat-Shock Proteins
0
HTT protein, human
0
Huntingtin Protein
0
Molecular Chaperones
0
Protein Aggregates
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
4692Informations de copyright
© 2022. The Author(s).
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