@article{HartmannWaiHuetal.2016,
  author    = {Hartmann, Bianca and Wai, Timothy and Hu, Hao and MacVicar, Thomas and Musante, Luciana and Fischer-Zirnsak, Bj{\"o}rn and Stenzel, Werner and Gr{\"a}f, Ralph and van den Heuvel, Lambert and Ropers, Hans-Hilger and Wienker, Thomas F. and H{\"u}bner, Christoph and Langer, Thomas and Kaindl, Angela M.},
  title     = {Homozygous YME1L1 Mutation Causes Mitochondriopathy with Optic Atrophy and Mitochondrial Network Fragmentation},
  series = {eLife},
  volume    = {5},
  journal   = {eLife},
  publisher = {eLife Sciences Publications},
  address   = {Cambridge},
  issn      = {2050-084X},
  doi       = {10.7554/eLife.16078},
  pages     = {1156 -- 1165},
  year      = {2016},
  abstract  = {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.},
  language  = {en}
}