Homozygous YME1L1 mutation causes mitochondriopathy with optic atrophy and mitochondrial network fragmentation
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Mitochondriopathies often present clinically as multisystemic disorders of primarily high-energy consuming organs. Assembly, turnover, and surveillance of mitochondrial proteins are essential for mitochondrial function and a key task of AAA family members of metalloproteases. We identified a homozygous mutation in the nuclear encoded mitochondrial escape 1-like 1 gene YME1L1, member of the AAA protease family, as a cause of a novel mitochondriopathy in a consanguineous pedigree of Saudi Arabian descent. The homozygous missense mutation, located in a highly conserved region in the mitochondrial pre-sequence, inhibits cleavage of YME1L1 by the mitochondrial processing peptidase, which culminates in the rapid degradation of YME1L1 precursor protein. Impaired YME1L1 function causes a proliferation defect and mitochondrial network fragmentation due to abnormal processing of OPA1. Our results identify mutations in YME1L1 as a cause of a mitochondriopathy with optic nerve atrophy highlighting the importance of YME1L1 for mitochondrial functionality in humans.
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Muscle biopsies from patients with YME1L1 mutation display alterations in cristae morphology, paracrystalline inclusions, and fiber-type grouping indicating denervation.
“Muscle biopsies from these patients display alterations in cristae morphology and paracrystalline inclusions and fiber-type grouping, indicating denervation [165].”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [165]
A homozygous missense mutation impairing IMS protease maturation of YME1L1 causes infantile onset mitochondriopathy with severe intellectual disability, muscular impairments, and optic nerve atrophy.
“The accumulation of damaged proteins due to a homozygous missense mutation that impairs the IMS protease maturation, YME1L1, causes infantile onset mitochondriopathy with severe intellectual disability, muscular impairments, and optic nerve atrophy.”
From The connection between the dynamic remodeling of the mitochondrial network and the regulation of muscle mass (2021) · cites this paper as [165]
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- Authors
- Hartmann, B., Wai, T., Hu, H., MacVicar, T., Musante, L., Fischer-Zirnsak, B., Stenzel, W., Gräf, R., van den Heuvel, L., Ropers, H.-H., Wienker, T. F., Hübner, C., Langer, T., & Kaindl, A. M.
- Affiliations
- Charité – Universitätsmedizin Berlin (DE)
- Cologne Excellence Cluster on Cellular Stress Responses in Aging Associated Diseases (DE)
- Guangzhou Women and Children Medical Center (CN)
- Max Planck Institute for Molecular Genetics (DE)
- Max Planck Institute for Molecular Genetics, Berlin, Germany
- University of Potsdam (DE)
- Nijmegen Center for Mitochondrial Disorders, Radboud University Medical Center, Nijmegen, Netherlands
- Corresponding author
- Kaindl, Angela M
- Venue
- eLife
- Publisher
- eLife Sciences Publications, Ltd
- Published
- 2016-08-06
- Volume
- 5
- ISSN
- 2050-084X (ISSN-L)
- PMC
- PMC4991934
- OpenAlex
- W2480597918
- Cited by
- 124
- References
- 50
- Citations by year
- 2026: 6 · 2025: 7 · 2024: 12 · 2023: 8 · 2022: 18 · 2021: 21 · 2020: 17 · 2019: 15 · 2018: 12 · 2017: 8
- FWCI
- 6.07
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- Locations
- eLife (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Kölner Universitäts PublikationsServer (Universität zu Köln) (publishedVersion)
- HAL (submittedVersion, other-oa)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Max Planck Digital Library (submittedVersion, other-oa)
- publish.UP (University of Potsdam) (submittedVersion)
- MPG.PuRe (Max Planck Society) (submittedVersion, cc-by)
- Refubium (Universitätsbibliothek der Freien Universität Berlin) (submittedVersion, cc-by)
- Radboud Repository (Radboud University) (submittedVersion)
- Radboud Repository (Radboud University) (submittedVersion, other-oa)
- Universitätsbibliothek der FU Berlin Hochschulschriftenstelle u. Dokumentenserver (cc-by)
- Funders
- Sonnenfeld Stiftung
- Deutsche Gesellschaft für Muskelkranke e.V.
- Human Frontier Science Program
- Max-Planck-Gesellschaft
- Deutsche Forschungsgemeinschaft (KO2891/1-1, Reinhart Koselleck Grant, SFB665)
- National Center for Research Resources (P20 RR016453)
- EU FP 7 project GENCODYS (241995)
- Berlin Institute of Health (BIH, CRG1)
- Deutscher Akademischer Austauschdienst
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Metabolism and Genetic Disorders
- Keywords
- optic atrophy, mitochondrial processing peptidase, mitochondrial presequence, consanguineous pedigree, missense mutations, protein degradation
- MeSH terms
- ATPases Associated with Diverse Cellular Activities, Female, Homozygote, Humans, Male, Metalloendopeptidases, Mitochondria, Optic Atrophy, Mutation, Missense, Mitochondrial Proteins, Mitochondrial Diseases
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