To aggregate or not to aggregate - Is it a matter of the ribosome?
aging
neurodegeneration
proteostasis
ribosome
translational fidelity
Journal
BioEssays : news and reviews in molecular, cellular and developmental biology
ISSN: 1521-1878
Titre abrégé: Bioessays
Pays: United States
ID NLM: 8510851
Informations de publication
Date de publication:
07 2023
07 2023
Historique:
revised:
05
05
2023
received:
01
12
2022
accepted:
05
05
2023
medline:
22
6
2023
pubmed:
17
5
2023
entrez:
17
5
2023
Statut:
ppublish
Résumé
Neurodegenerative syndromes present as proteinopathies - does ribosomal infidelity contribute to the protein toxicity that is the driving force for neuronal cell loss? Intracellular and extracellular protein aggregates overwhelm the clearance capacity of cells and tissues. Proteins aggregate when hydrophobic residues are exposed. Hydrophobic residues become exposed when proteins are misfolded. Protein misfolding can originate from translational errors at the ribosome. Indeed, the most error-prone process in gene expression is translation at the ribosome. Recent evidence indicates that manipulating the ribosomal accuracy impacts on the lifespan of model organisms and a reduced translational accuracy is accompanied by neurodegeneration. The first hit in aging-associated neurodegenerative disease may be the well-documented decline of cellular buffering capacity by aging. A second hit that impacts on the quality of protein synthesis could be the driving force for the observed loss of proteostasis in neurodegeneration. This hypothesis provides an explanation for the late onset of most neurodegenerative diseases.
Identifiants
pubmed: 37194995
doi: 10.1002/bies.202200230
doi:
Substances chimiques
Proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e2200230Commentaires et corrections
Type : CommentIn
Informations de copyright
© 2023 The Authors. BioEssays published by Wiley Periodicals LLC.
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