LON is the master protease that protects against protein aggregation in human mitochondria through direct degradation of misfolded proteins
Open accessAbstract
Maintenance of mitochondrial protein homeostasis is critical for proper cellular function. Under normal conditions resident molecular chaperones and proteases maintain protein homeostasis within the organelle. Under conditions of stress however, misfolded proteins accumulate leading to the activation of the mitochondrial unfolded protein response (UPR mt). While molecular chaperone assisted refolding of proteins in mammalian mitochondria has been well documented, the contribution of AAA+ proteases to the maintenance of protein homeostasis in this organelle remains unclear. To address this gap in knowledge we examined the contribution of human mitochondrial matrix proteases, LONM and CLPXP, to the turnover of OTC-∆, a folding incompetent mutant of ornithine transcarbamylase, known to activate UPR mt. Contrary to a model whereby CLPXP is believed to degrade misfolded proteins, we found that LONM and not CLPXP is responsible for the turnover of OTC-∆ in human mitochondria. To analyse the conformational state of proteins that are recognised by LONM, we examined the turnover of unfolded and aggregated forms of malate dehydrogenase (MDH) and OTC. This analysis revealed that LONM specifically recognises and degrades unfolded, but not aggregated proteins. Since LONM is not upregulated by UPR mt, this pathway may preferentially act to promote chaperone mediated refolding of proteins.
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LONP1 degrades ΔOTC.
“Consistent with LONP1 degrading ΔOTC39,40”
From Disuse-associated loss of the protease Lonp1 in muscle impairs mitochondrial function and causes reduced skeletal muscle mass and strength (2022) · cites this paper as [40]
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- Authors
- Bezawork-Geleta, A., Brodie, E. J., Dougan, D. A., & Truscott, K. N.
- Affiliations
- La Trobe University (AU)
- Corresponding author
- Dougan, David A.
- Truscott, Kaye N.
- Venue
- Scientific Reports
- Published
- 2015-12-02
- Volume
- 5
- Issue
- 1
- Pages
- 17397-17397
- ISSN
- 2045-2322 (ISSN-L)
- PMC
- PMC4667172
- OpenAlex
- W2444473506
- Cited by
- 113
- References
- 78
- Citations by year
- 2026: 9 · 2025: 6 · 2024: 7 · 2023: 5 · 2022: 15 · 2021: 10 · 2020: 20 · 2019: 11 · 2018: 8 · 2017: 10 · 2016: 12
- FWCI
- 4.34
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Scientific Reports (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Minerva Access (University of Melbourne) (submittedVersion, cc-by)
- Griffith Research Online (submittedVersion, cc-by)
- Funders
- La Trobe University
- Monash University
- Australian Research Council (DP110103936, FT0992033)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Keywords
- Lon protease, mitochondrial matrix protease, ClpXP, mitochondrial protein homeostasis, protein aggregation, mitochondrial unfolded protein response, misfolded protein degradation, ornithine transcarbamylase, malate dehydrogenase, AAA+ protease, protein turnover
- MeSH terms
- Animals, HeLa Cells, Humans, Mitochondria, Mitochondrial Proteins, Protease La, Endopeptidase Clp, Rats, Unfolded Protein Response, Proteolysis, Protein Aggregates
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