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@ARTICLE{Grossmann:265796,
      author       = {Grossmann, Dajana and Malburg, Nina and Glaß, Hannes and
                      Weeren, Veronika and Sondermann, Verena and Pfeiffer, Julia
                      F and Petters, Janine and Lukas, Jan and Seibler, Philip and
                      Klein, Christine and Grünewald, Anne and Hermann, Andreas},
      title        = {{M}itochondria-{E}ndoplasmic {R}eticulum {C}ontact {S}ites
                      {D}ynamics and {C}alcium {H}omeostasis {A}re
                      {D}ifferentially {D}isrupted in {PINK}1-{PD} or {PRKN}-{PD}
                      {N}eurons.},
      journal      = {Movement disorders},
      volume       = {38},
      number       = {10},
      issn         = {0885-3185},
      address      = {New York, NY},
      publisher    = {Wiley},
      reportid     = {DZNE-2023-01040},
      pages        = {1822 - 1836},
      year         = {2023},
      abstract     = {It is generally believed that the pathogenesis of
                      PINK1/parkin-related Parkinson's disease (PD) is due to a
                      disturbance in mitochondrial quality control. However,
                      recent studies have found that PINK1 and Parkin play a
                      significant role in mitochondrial calcium homeostasis and
                      are involved in the regulation of mitochondria-endoplasmic
                      reticulum contact sites (MERCSs).The aim of our study was to
                      perform an in-depth analysis of the role of MERCSs and
                      impaired calcium homeostasis in PINK1/Parkin-linked PD.In
                      our study, we used induced pluripotent stem cell-derived
                      dopaminergic neurons from patients with PD with
                      loss-of-function mutations in PINK1 or PRKN. We employed a
                      split-GFP-based contact site sensor in combination with the
                      calcium-sensitive dye Rhod-2 AM and applied Airyscan
                      live-cell super-resolution microscopy to determine how
                      MERCSs are involved in the regulation of mitochondrial
                      calcium homeostasis.Our results showed that
                      thapsigargin-induced calcium stress leads to an increase of
                      the abundance of narrow MERCSs in wild-type neurons.
                      Intriguingly, calcium levels at the MERCSs remained stable,
                      whereas the increased net calcium influx resulted in
                      elevated mitochondrial calcium levels. However, PINK1-PD or
                      PRKN-PD neurons showed an increased abundance of MERCSs at
                      baseline, accompanied by an inability to further increase
                      MERCSs upon thapsigargin-induced calcium stress.
                      Consequently, calcium distribution at MERCSs and within
                      mitochondria was disrupted.Our results demonstrated how the
                      endoplasmic reticulum and mitochondria work together to cope
                      with calcium stress in wild-type neurons. In addition, our
                      results suggests that PRKN deficiency affects the dynamics
                      and composition of MERCSs differently from PINK1 deficiency,
                      resulting in differentially affected calcium homeostasis. ©
                      2023 The Authors. Movement Disorders published by Wiley
                      Periodicals LLC on behalf of International Parkinson and
                      Movement Disorder Society.},
      keywords     = {Humans / Parkinson Disease: pathology / Calcium: metabolism
                      / Thapsigargin: metabolism / Mitochondria: pathology /
                      Dopaminergic Neurons: metabolism / Protein Kinases: genetics
                      / Ubiquitin-Protein Ligases: genetics / Endoplasmic
                      Reticulum: metabolism / Homeostasis / PTEN-induced putative
                      kinase (NLM Chemicals) / PINK1 (Other) / Parkin (Other) /
                      Parkinson's disease (Other) / calcium (Other) /
                      mitochondria-ER contact sites (Other) / Calcium (NLM
                      Chemicals) / Thapsigargin (NLM Chemicals) / Protein Kinases
                      (NLM Chemicals) / Ubiquitin-Protein Ligases (NLM Chemicals)
                      / parkin protein (NLM Chemicals)},
      cin          = {AG Hermann},
      ddc          = {610},
      cid          = {I:(DE-2719)1511100},
      pnm          = {353 - Clinical and Health Care Research (POF4-353)},
      pid          = {G:(DE-HGF)POF4-353},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:37449534},
      doi          = {10.1002/mds.29525},
      url          = {https://pub.dzne.de/record/265796},
}