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@ARTICLE{Baden:257563,
      author       = {Baden, Pascale and Perez, Maria Jose and Raji, Hariam and
                      Bertoli, Federico and Kalb, Stefanie and Illescas, María
                      and Spanos, Fokion and Giuliano, Claudio and Calogero,
                      Alessandra Maria and Oldrati, Marvin and Hebestreit, Hannah
                      and Cappelletti, Graziella and Brockmann, Kathrin and
                      Gasser, Thomas and Schapira, Anthony H V and Ugalde,
                      Cristina and Deleidi, Michela},
      title        = {{G}lucocerebrosidase is imported into mitochondria and
                      preserves complex {I} integrity and energy metabolism.},
      journal      = {Nature Communications},
      volume       = {14},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {DZNE-2023-00443},
      pages        = {1930},
      year         = {2023},
      abstract     = {Mutations in GBA1, the gene encoding the lysosomal enzyme
                      β-glucocerebrosidase (GCase), which cause Gaucher's
                      disease, are the most frequent genetic risk factor for
                      Parkinson's disease (PD). Here, we employ global proteomic
                      and single-cell genomic approaches in stable cell lines as
                      well as induced pluripotent stem cell (iPSC)-derived neurons
                      and midbrain organoids to dissect the mechanisms underlying
                      GCase-related neurodegeneration. We demonstrate that GCase
                      can be imported from the cytosol into the mitochondria via
                      recognition of internal mitochondrial targeting
                      sequence-like signals. In mitochondria, GCase promotes the
                      maintenance of mitochondrial complex I (CI) integrity and
                      function. Furthermore, GCase interacts with the
                      mitochondrial quality control proteins HSP60 and LONP1.
                      Disease-associated mutations impair CI stability and
                      function and enhance the interaction with the mitochondrial
                      quality control machinery. These findings reveal a
                      mitochondrial role of GCase and suggest that defective CI
                      activity and energy metabolism may drive the pathogenesis of
                      GCase-linked neurodegeneration.},
      keywords     = {Humans / Glucosylceramidase: genetics / Glucosylceramidase:
                      metabolism / Proteomics / Parkinson Disease: metabolism /
                      Mitochondria: genetics / Mitochondria: metabolism / Energy
                      Metabolism: genetics / Mutation / Lysosomes: metabolism /
                      alpha-Synuclein: metabolism / Mitochondrial Proteins:
                      metabolism / ATP-Dependent Proteases: metabolism /
                      Glucosylceramidase (NLM Chemicals) / alpha-Synuclein (NLM
                      Chemicals) / LONP1 protein, human (NLM Chemicals) /
                      Mitochondrial Proteins (NLM Chemicals) / ATP-Dependent
                      Proteases (NLM Chemicals)},
      cin          = {AG Deleidi / AG Gasser 1},
      ddc          = {500},
      cid          = {I:(DE-2719)1210011 / I:(DE-2719)1210000},
      pnm          = {352 - Disease Mechanisms (POF4-352) / 353 - Clinical and
                      Health Care Research (POF4-353)},
      pid          = {G:(DE-HGF)POF4-352 / G:(DE-HGF)POF4-353},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37024507},
      pmc          = {pmc:PMC10079970},
      doi          = {10.1038/s41467-023-37454-4},
      url          = {https://pub.dzne.de/record/257563},
}