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@ARTICLE{Chiang:280915,
      author       = {Chiang, Claire Y and Pratuseviciute, Neringa and Lin, Yu-En
                      and Adhikari, Ayan and Yeshaw, Wondwossen M and Flitton,
                      Chloe and Sherpa, Pemba L and Tonelli, Francesca and
                      Rektorova, Irena and Lynch, Timothy and Siuda, Joanna and
                      Rudzińska-Bar, Monika and Pulyk, Oleksandr and Bauer, Peter
                      and Beetz, Christian and Dickson, Dennis W and Ross, Owen A
                      and Wszolek, Zbigniew K and Fang, Zih-Hua and Klein,
                      Christine and Zimprich, Alexander and Alessi, Dario R and
                      Sammler, Esther M and Pfeffer, Suzanne R},
      collaboration = {Program, Global Parkinson’s Genetics},
      title        = {{PPM}1{M}, an {LRRK}2-counteracting,
                      phospho{R}ab12-preferring phosphatase with a potential link
                      to {P}arkinson's disease.},
      journal      = {Cell reports},
      volume       = {44},
      number       = {8},
      issn         = {2211-1247},
      address      = {Maryland Heights, MO},
      publisher    = {Cell Press},
      reportid     = {DZNE-2025-00998},
      pages        = {116031 -},
      year         = {2025},
      abstract     = {Leucine-rich repeat kinase 2 (LRRK2) phosphorylates a
                      subset of Rab GTPases that regulate receptor trafficking,
                      and LRRK2-activating mutations are linked to Parkinson's
                      disease. Rab phosphorylation is a transient event that can
                      be reversed by phosphatases, including protein phosphatase,
                      Mg2+/Mn2+ dependent 1H (PPM1H), which acts on phosphorylated
                      Rab 8A (phosphoRab8A) and phosphoRab10. Here, we report a
                      phosphatome-wide small interfering RNA (siRNA) screen that
                      identified PPM1M as a phosphoRab12-preferring phosphatase
                      that also acts on phosphoRab8A and phosphoRab10. Upon
                      knockout from cultured cells or mice, PPM1M displays
                      selectivity for phosphoRab12. As shown previously for mice
                      harboring LRRK2 pathway mutations, knockout of Ppm1m leads
                      to primary cilia loss in striatal cholinergic and
                      parvalbumin interneurons. We also identified a rare PPM1M
                      mutation in patients with Parkinson's disease that is
                      catalytically inactive when tested in vitro and in cells.
                      These findings identify PPM1M as a key player in the LRRK2
                      signaling pathway and provide a new therapeutic target for
                      the possible benefit of patients with Parkinson's disease.},
      keywords     = {Parkinson Disease: metabolism / Parkinson Disease: genetics
                      / Parkinson Disease: pathology / Leucine-Rich Repeat
                      Serine-Threonine Protein Kinase-2: metabolism / Leucine-Rich
                      Repeat Serine-Threonine Protein Kinase-2: genetics / Animals
                      / Humans / Mice / rab GTP-Binding Proteins: metabolism /
                      Phosphorylation / HEK293 Cells / Protein Phosphatase 2C:
                      metabolism / Protein Phosphatase 2C: genetics / Mutation /
                      Mice, Knockout / CP: Cell biology (Other) / CP: Neuroscience
                      (Other) / LRRK2 kinase (Other) / Parkinson’s disease
                      (Other) / Rab GTPase (Other) / phosphatase (Other) / primary
                      cilia (Other) / Leucine-Rich Repeat Serine-Threonine Protein
                      Kinase-2 (NLM Chemicals) / rab GTP-Binding Proteins (NLM
                      Chemicals) / Protein Phosphatase 2C (NLM Chemicals)},
      cin          = {AG Heutink},
      ddc          = {610},
      cid          = {I:(DE-2719)1210002},
      pnm          = {354 - Disease Prevention and Healthy Aging (POF4-354)},
      pid          = {G:(DE-HGF)POF4-354},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40690364},
      doi          = {10.1016/j.celrep.2025.116031},
      url          = {https://pub.dzne.de/record/280915},
}