Digest it all: the lysosomal turnover of cytoplasmic aggregates.
cellular protein quality control
chaperone-mediated autophagy
macro-autophagy
micro-autophagy
p62 bodies
selective autophagy receptors
Journal
Trends in biochemical sciences
ISSN: 0968-0004
Titre abrégé: Trends Biochem Sci
Pays: England
ID NLM: 7610674
Informations de publication
Date de publication:
03 2023
03 2023
Historique:
received:
15
07
2022
revised:
29
09
2022
accepted:
29
09
2022
pubmed:
25
10
2022
medline:
25
2
2023
entrez:
24
10
2022
Statut:
ppublish
Résumé
Aggrephagy describes the selective lysosomal transport and turnover of cytoplasmic protein aggregates by macro-autophagy. In this process, protein aggregates and conglomerates are polyubiquitinated and then sequestered by autophagosomes. Soluble selective autophagy receptors (SARs) are central to aggrephagy and physically bind to both ubiquitin and the autophagy machinery, thus linking the cargo to the forming autophagosomal membrane. Because the accumulation of protein aggregates is associated with cytotoxicity in several diseases, a better molecular understanding of aggrephagy might provide a conceptual framework to develop therapeutic strategies aimed at delaying the onset of these pathologies by preventing the buildup of potentially toxic aggregates. We review recent advances in our knowledge about the mechanism of aggrephagy.
Identifiants
pubmed: 36280494
pii: S0968-0004(22)00271-7
doi: 10.1016/j.tibs.2022.09.012
pii:
doi:
Substances chimiques
Sequestosome-1 Protein
0
Protein Aggregates
0
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
216-228Informations de copyright
Copyright © 2022 The Authors. Published by Elsevier Ltd.. All rights reserved.
Déclaration de conflit d'intérêts
Declaration of interests The authors declare no conflicts of interest.