Mitochondrial matrix proteases: quality control and beyond.
ClpXP
LONP1
metabolism
mitochondria
mitochondrial matrix proteases
protein quality control
regulated proteolysis
respiratory chain complexes
Journal
The FEBS journal
ISSN: 1742-4658
Titre abrégé: FEBS J
Pays: England
ID NLM: 101229646
Informations de publication
Date de publication:
11 2022
11 2022
Historique:
revised:
22
03
2021
received:
18
11
2020
accepted:
07
05
2021
pubmed:
11
5
2021
medline:
18
11
2022
entrez:
10
5
2021
Statut:
ppublish
Résumé
To ensure correct function, mitochondria have developed several mechanisms of protein quality control (QC). Protein homeostasis highly relies on chaperones and proteases to maintain proper folding and remove damaged proteins that might otherwise form cell-toxic aggregates. Besides quality control, mitochondrial proteases modulate and regulate many essential functions, such as trafficking, processing and activation of mitochondrial proteins, mitochondrial dynamics, mitophagy and apoptosis. Therefore, the impaired function of mitochondrial proteases is associated with various pathological conditions, including cancer, metabolic syndromes and neurodegenerative disorders. This review recapitulates and discusses the emerging roles of two major proteases of the mitochondrial matrix, LON and ClpXP. Although commonly acknowledge for their protein quality control role, recent advances have uncovered several highly regulated processes controlled by the LON and ClpXP connected to mitochondrial gene expression and respiratory chain function maintenance. Furthermore, both proteases have been lately recognized as potent targets for anticancer therapies, and we summarize those findings.
Substances chimiques
Peptide Hydrolases
EC 3.4.-
Mitochondrial Proteins
0
Molecular Chaperones
0
Endopeptidases
EC 3.4.-
Types de publication
Journal Article
Review
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
7128-7146Informations de copyright
© 2021 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies.
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