Defective mitochondrial protease LonP1 can cause classical mitochondrial disease
Open accessAbstract
LonP1 is a mitochondrial matrix protease whose selective substrate specificity is essential for maintaining mitochondrial homeostasis. Recessively inherited, pathogenic defects in LonP1 have been previously reported to underlie cerebral, ocular, dental, auricular and skeletal anomalies (CODAS) syndrome, a complex multisystemic and developmental disorder. Intriguingly, although classical mitochondrial disease presentations are well-known to exhibit marked clinical heterogeneity, the skeletal and dental features associated with CODAS syndrome are pathognomonic. We have applied whole exome sequencing to a patient with congenital lactic acidosis, muscle weakness, profound deficiencies in mitochondrial oxidative phosphorylation associated with loss of mtDNA copy number and MRI abnormalities consistent with Leigh syndrome, identifying biallelic variants in the LONP1 (NM_004793.3) gene; c.1693T > C predicting p.(Tyr565His) and c.2197G > A predicting p.(Glu733Lys); no evidence of the classical skeletal or dental defects observed in CODAS syndrome patients were noted in our patient. In vitro experiments confirmed the p.(Tyr565His) LonP1 mutant alone could not bind or degrade a substrate, consistent with the predicted function of Tyr565, whilst a second missense [p.(Glu733Lys)] variant had minimal effect. Mixtures of p.(Tyr565His) mutant and wild-type LonP1 retained partial protease activity but this was severely depleted when the p.(Tyr565His) mutant was mixed with the p.(Glu733Lys) mutant, data consistent with the compound heterozygosity detected in our patient. In summary, we conclude that pathogenic LONP1 variants can lead to a classical mitochondrial disease presentations associated with severe biochemical defects in oxidative phosphorylation in clinically relevant tissues.
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In human skeletal muscle, reduction of LonP1 activity results in electron-dense intra-mitochondrial accumulations, mitochondrial dysfunction, oxidative stress, and muscle weakness.
“In human skeletal muscle, the reduction of LonP1 activity results in electron-dense intra-mitochondrial accumulations, mitochondrial dysfunction, oxidative stress, and muscle weakness [162–164].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [162]
The matrix mitochondrial protease LonP1 is necessary for maintenance of mitochondrial matrix proteostasis.
“The matrix mitochondrial protease LonP1 is necessary for the maintenance of mitochondrial matrix proteostasis.”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [162]
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Mitochondrial protease and human disease
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Beyond the genome: clinical challenges in diagnosing LONP1-related mitochondrial disorders
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- Authors
- Peter, B., Waddington, C. L., Oláhová, M., Sommerville, E. W., Hopton, S., Pyle, A., Champion, M., Ohlson, M., Siibak, T., Chrzanowska-Lightowlers, Z. M. A., Taylor, R. W., Falkenberg, M., & Lightowlers, R. N.
- Affiliations
- University of Gothenburg (SE)
- Wellcome Centre for Mitochondrial Research (GB)
- Baylor College of Medicine (US)
- Guy's and St Thomas' NHS Foundation Trust (GB)
- Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, TX, USA
- Corresponding author
- Lightowlers, Robert N
- ORCID
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2018-03-06
- Volume
- 27
- Issue
- 10
- Pages
- 1743-1753
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- PMC
- PMC5932559
- OpenAlex
- W2793194148
- Cited by
- 66
- References
- 28
- Citations by year
- 2026: 6 · 2025: 9 · 2024: 8 · 2023: 7 · 2022: 5 · 2021: 14 · 2020: 10 · 2019: 4 · 2018: 3
- FWCI
- 2.76
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Human Molecular Genetics (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Swedish Research Council (2013–3621)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genomics and Rare Diseases
- Keywords
- LONP1, mitochondrial matrix protease, mitochondrial disease, Leigh syndrome, compound heterozygosity, missense mutations, oxidative phosphorylation deficiency, mitochondrial DNA copy number, congenital lactic acidosis, protease specificity
- MeSH terms
- Exome Sequencing, Biopsy, Cell Line, Eye Abnormalities, Growth Disorders, Hip Dislocation, Congenital, Humans, Infant, Leigh Disease, Male, Mitochondria, Mutation, Osteochondrodysplasias, Oxidative Phosphorylation, Tooth Abnormalities, Muscle, Skeletal, Craniofacial Abnormalities, Mitochondrial Proteins, Mitochondrial Diseases, ATP-Dependent Proteases, Exome
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