HSPB8 frameshift mutant aggregates weaken chaperone-assisted selective autophagy in neuromyopathies.
Humans
Sequestosome-1 Protein
/ genetics
Autophagy
/ genetics
Heat-Shock Proteins
/ metabolism
Neuromuscular Diseases
Charcot-Marie-Tooth Disease
/ genetics
Ubiquitin-Protein Ligases
/ metabolism
Adaptor Proteins, Signal Transducing
/ metabolism
Apoptosis Regulatory Proteins
/ metabolism
Molecular Chaperones
/ genetics
BAG3
CASA
HSPA
HSPB8
misfolding
myopathy
neuromuscular disorders
neuropathy
protein quality control
Journal
Autophagy
ISSN: 1554-8635
Titre abrégé: Autophagy
Pays: United States
ID NLM: 101265188
Informations de publication
Date de publication:
08 2023
08 2023
Historique:
medline:
17
7
2023
pubmed:
1
3
2023
entrez:
28
2
2023
Statut:
ppublish
Résumé
Chaperone-assisted selective autophagy (CASA) is a highly selective pathway for the disposal of misfolding and aggregating proteins. In muscle, CASA assures muscle integrity by favoring the turnover of structural components damaged by mechanical strain. In neurons, CASA promotes the removal of aggregating substrates. A crucial player of CASA is HSPB8 (heat shock protein family B (small) member 8), which acts in a complex with HSPA, their cochaperone BAG3, and the E3 ubiquitin ligase STUB1. Recently, four novel
Identifiants
pubmed: 36854646
doi: 10.1080/15548627.2023.2179780
pmc: PMC10351472
doi:
Substances chimiques
Sequestosome-1 Protein
0
Heat-Shock Proteins
0
STUB1 protein, human
EC 2.3.2.27
Ubiquitin-Protein Ligases
EC 2.3.2.27
BAG3 protein, human
0
Adaptor Proteins, Signal Transducing
0
Apoptosis Regulatory Proteins
0
HSPB8 protein, human
0
Molecular Chaperones
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2217-2239Références
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