Ubiquitin Signaling and Degradation of Aggregate-Prone Proteins.
E3 ubiquitin ligase
autophagy
deubiquitylating enzyme
neurodegenerative diseases
proteasome
Journal
Trends in biochemical sciences
ISSN: 0968-0004
Titre abrégé: Trends Biochem Sci
Pays: England
ID NLM: 7610674
Informations de publication
Date de publication:
10 2019
10 2019
Historique:
received:
03
02
2019
revised:
08
04
2019
accepted:
11
04
2019
pubmed:
14
5
2019
medline:
28
7
2020
entrez:
14
5
2019
Statut:
ppublish
Résumé
Mutant protein aggregation and misfolding is often correlated with toxicity in neurodegenerative diseases. Aggregate-prone proteins are tagged by ubiquitin that signals them for destruction by the proteasome or autophagy, two key pathways for protein degradation and proteostasis. Here, we review recent studies showing that the regulation of aggregate-prone proteins by ubiquitin signaling is more complex than initially postulated. We discuss how the ubiquitin code of aggregate-prone proteins is written by specific E3 ubiquitin ligases and edited by deubiquitylating enzymes (DUBs) in cells and in brain tissues, as well as how this affects protein degradation. These studies have advanced our understanding of the specificity of the ubiquitin system and provide new information about its relevance to neurodegenerative diseases and therapy.
Identifiants
pubmed: 31079890
pii: S0968-0004(19)30087-8
doi: 10.1016/j.tibs.2019.04.007
pii:
doi:
Substances chimiques
Protein Aggregates
0
Proteins
0
Ubiquitin
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
872-884Informations de copyright
Copyright © 2019 Elsevier Ltd. All rights reserved.