Universität zu Köln

Szczepanowska, Karolina ORCID: 0000-0003-4689-2350 and Trifunovic, Aleksandra ORCID: 0000-0002-5472-3517 . Mitochondrial matrix proteases: quality control and beyond. FEBS J.. HOBOKEN: WILEY. ISSN 1742-4658

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Abstract

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.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Szczepanowska, Karolina UNSPECIFIED orcid.org/0000-0003-4689-2350 UNSPECIFIED Trifunovic, Aleksandra UNSPECIFIED orcid.org/0000-0002-5472-3517 UNSPECIFIED
URN:	urn:nbn:de:hbz:38-565539
DOI:	10.1111/febs.15964
Journal or Publication Title:	FEBS J.
Publisher:	WILEY
Place of Publication:	HOBOKEN
ISSN:	1742-4658
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language DEPENDENT LON PROTEASE; CLPP SERINE-PROTEASE; TRANSCRIPTION FACTOR; CANCER-CELLS; COMPLEX-I; MOLECULAR CHAPERONES; PROMOTES DEGRADATION; THERAPEUTIC STRATEGY; MISFOLDED PROTEINS; CRYSTAL-STRUCTURE Multiple languages Biochemistry & Molecular Biology Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/56553