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@ARTICLE{Rolland:137010,
      author       = {Rolland, Stéphane G and Motori, Elisa and Memar, Nadin and
                      Hench, Jürgen and Frank, Stephan and Winklhofer, Konstanze
                      F and Conradt, Barbara},
      title        = {{I}mpaired complex {IV} activity in response to loss of
                      {LRPPRC} function can be compensated by mitochondrial
                      hyperfusion.},
      journal      = {Proceedings of the National Academy of Sciences of the
                      United States of America},
      volume       = {110},
      number       = {32},
      issn         = {0027-8424},
      address      = {Washington, DC},
      publisher    = {National Acad. of Sciences},
      reportid     = {DZNE-2020-03332},
      pages        = {E2967-E2976},
      year         = {2013},
      abstract     = {Mitochondrial morphology changes in response to various
                      stimuli but the significance of this is unclear. In a screen
                      for mutants with abnormal mitochondrial morphology, we
                      identified MMA-1, the Caenorhabditis elegans homolog of the
                      French Canadian Leigh Syndrome protein LRPPRC (leucine-rich
                      pentatricopeptide repeat containing). We demonstrate that
                      reducing mma-1 or LRPPRC function causes mitochondrial
                      hyperfusion. Reducing mma-1/LRPPRC function also decreases
                      the activity of complex IV of the electron transport chain,
                      however without affecting cellular ATP levels. Preventing
                      mitochondrial hyperfusion in mma-1 animals causes larval
                      arrest and embryonic lethality. Furthermore, prolonged
                      LRPPRC knock-down in mammalian cells leads to mitochondrial
                      fragmentation and decreased levels of ATP. These findings
                      indicate that in a mma-1/LRPPRC-deficient background,
                      hyperfusion allows mitochondria to maintain their functions
                      despite a reduction in complex IV activity. Our data reveal
                      an evolutionary conserved mechanism that is triggered by
                      reduced complex IV function and that induces mitochondrial
                      hyperfusion to transiently compensate for a drop in the
                      activity of the electron transport chain.},
      keywords     = {Adenosine Triphosphate: metabolism / Animals / Animals,
                      Genetically Modified / Blotting, Western / Caenorhabditis
                      elegans: genetics / Caenorhabditis elegans: metabolism /
                      Caenorhabditis elegans Proteins: genetics / Caenorhabditis
                      elegans Proteins: metabolism / Cell Line / Cell Line, Tumor
                      / DNA-Binding Proteins: genetics / DNA-Binding Proteins:
                      metabolism / Electron Transport Complex IV: metabolism / GTP
                      Phosphohydrolases: genetics / GTP Phosphohydrolases:
                      metabolism / Green Fluorescent Proteins: genetics / Green
                      Fluorescent Proteins: metabolism / Humans / Leigh Disease:
                      genetics / Leigh Disease: metabolism / Leigh Disease:
                      pathology / Membrane Proteins: genetics / Membrane Proteins:
                      metabolism / Microscopy, Fluorescence / Mitochondria:
                      genetics / Mitochondria: metabolism / Mitochondrial
                      Proteins: genetics / Mitochondrial Proteins: metabolism /
                      Neoplasm Proteins: genetics / Neoplasm Proteins: metabolism
                      / RNA Interference / Transcription Factors: genetics /
                      Transcription Factors: metabolism / Caenorhabditis elegans
                      Proteins (NLM Chemicals) / DNA-Binding Proteins (NLM
                      Chemicals) / LRPPRC protein, human (NLM Chemicals) / MMA-1
                      protein, C elegans (NLM Chemicals) / Membrane Proteins (NLM
                      Chemicals) / Mitochondrial Proteins (NLM Chemicals) /
                      Neoplasm Proteins (NLM Chemicals) / SCO1 protein, human (NLM
                      Chemicals) / TFAM protein, human (NLM Chemicals) /
                      Transcription Factors (NLM Chemicals) / Green Fluorescent
                      Proteins (NLM Chemicals) / Adenosine Triphosphate (NLM
                      Chemicals) / Electron Transport Complex IV (NLM Chemicals) /
                      GTP Phosphohydrolases (NLM Chemicals) / OPA1 protein, human
                      (NLM Chemicals)},
      cin          = {AG Winklhofer},
      ddc          = {500},
      cid          = {I:(DE-2719)5000047},
      pnm          = {341 - Molecular Signaling (POF3-341)},
      pid          = {G:(DE-HGF)POF3-341},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23878239},
      pmc          = {pmc:PMC3740885},
      doi          = {10.1073/pnas.1303872110},
      url          = {https://pub.dzne.de/record/137010},
}