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@ARTICLE{Park:165146,
      author       = {Park, Jae-Sook and Hu, Yiying and Hollingsworth, Nancy M
                      and Miltenberger-Miltenyi, Gabriel and Neiman, Aaron M},
      title        = {{I}nteraction between {VPS}13{A} and the {XK} scramblase is
                      important for {VPS}13{A} function in humans.},
      journal      = {Journal of cell science},
      volume       = {135},
      number       = {17},
      issn         = {0021-9533},
      address      = {Cambridge},
      publisher    = {Company of Biologists Limited},
      reportid     = {DZNE-2022-01451},
      pages        = {jcs260227},
      year         = {2022},
      abstract     = {VPS13 family proteins form conduits between the membranes
                      of different organelles through which lipids are
                      transferred. In humans, there are four VPS13 paralogs, and
                      mutations in the genes encoding each of them are associated
                      with different inherited disorders. VPS13 proteins contain
                      multiple conserved domains. The Vps13 adaptor-binding (VAB)
                      domain binds to adaptor proteins that recruit VPS13 to
                      specific membrane contact sites. This work demonstrates the
                      importance of a different domain in VPS13A function. The
                      pleckstrin homology (PH) domain at the C-terminal region of
                      VPS13A is required to form a complex with the XK scramblase
                      and for the co-localization of VPS13A with XK within the
                      cell. Alphafold modeling was used to predict an interaction
                      surface between VPS13A and XK. Mutations in this region
                      disrupt both complex formation and co-localization of the
                      two proteins. Mutant VPS13A alleles found in patients with
                      VPS13A disease truncate the PH domain. The phenotypic
                      similarities between VPS13A disease and McLeod syndrome
                      caused by mutations in VPS13A and XK, respectively, argue
                      that loss of the VPS13A-XK complex is the basis of both
                      diseases.},
      keywords     = {Humans / Mitochondrial Membranes: metabolism / Mutation:
                      genetics / Neuroacanthocytosis: complications /
                      Neuroacanthocytosis: genetics / Neuroacanthocytosis:
                      metabolism / Vesicular Transport Proteins: genetics /
                      Vesicular Transport Proteins: metabolism / Lipid transport
                      (Other) / Neuro-acanthocytosis syndromes (Other) /
                      Neurodegeneration (Other) / PH domain (Other) / VPS13A
                      (Other) / XK (Other) / VPS13A protein, human (NLM Chemicals)
                      / Vesicular Transport Proteins (NLM Chemicals)},
      cin          = {Zebrafish Models ; AG Schmid München},
      ddc          = {570},
      cid          = {I:(DE-2719)1140002},
      pnm          = {353 - Clinical and Health Care Research (POF4-353)},
      pid          = {G:(DE-HGF)POF4-353},
      typ          = {PUB:(DE-HGF)16},
      pmc          = {pmc:PMC9482346},
      pubmed       = {pmid:35950506},
      doi          = {10.1242/jcs.260227},
      url          = {https://pub.dzne.de/record/165146},
}