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@ARTICLE{Held:274095,
      author       = {Held, Sebastian and Erck, Christian and Kemppainen, Susanna
                      and Bleibaum, Florian and Giridhar, Neha Jadhav and
                      Feederle, Regina and Krenner, Claudia and Juopperi,
                      Sini-Pauliina and Calliari, Anna and Mentrup, Torben and
                      Schröder, Bernd and Dickson, Dennis W. and Rauramaa, Tuomas
                      and Petrucelli, Leonard and Prudencio, Mercedes and
                      Hiltunen, Mikko and Lüningschrör, Patrick and Capell, Anja
                      and Damme, Markus},
      title        = {{P}hysiological shedding and {C}-terminal proteolytic
                      processing of {TMEM}106{B}},
      journal      = {Cell reports},
      volume       = {44},
      number       = {1},
      issn         = {2211-1247},
      address      = {[New York, NY]},
      publisher    = {Elsevier},
      reportid     = {DZNE-2025-00051},
      pages        = {115107},
      year         = {2025},
      abstract     = {Genetic variants in TMEM106B, coding for a transmembrane
                      protein of unknown function, have been identified as
                      critical genetic modulators in various neurodegenerative
                      diseases with a strong effect in patients with
                      frontotemporal degeneration. The luminal domain of TMEM106B
                      can form amyloid-like fibrils upon proteolysis. Whether this
                      luminal domain is generated under physiological conditions
                      and which protease(s) are involved in shedding remain
                      unclear. We developed a commercially available antibody
                      against the luminal domain of TMEM106B, allowing a detailed
                      survey of the proteolytic processing under physiological
                      conditions in cellular models and TMEM106B-related mouse
                      models. Moreover, fibrillary TMEM106B was detected in human
                      autopsy material. We find that the luminal domain is
                      generated by multiple lysosomal cysteine-type proteases.
                      Cysteine-type proteases perform additional C-terminal
                      trimming, for which experimental evidence has been lacking.
                      The presented results allow an in-depth perception of the
                      processing of TMEM106B, a prerequisite to understanding
                      factors leading to fibril formation.},
      cin          = {AG Feederle / AG Haass},
      ddc          = {610},
      cid          = {I:(DE-2719)1140004 / I:(DE-2719)1110007},
      pnm          = {352 - Disease Mechanisms (POF4-352) / 899 - ohne Topic
                      (POF4-899)},
      pid          = {G:(DE-HGF)POF4-352 / G:(DE-HGF)POF4-899},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39709600},
      doi          = {10.1016/j.celrep.2024.115107},
      url          = {https://pub.dzne.de/record/274095},
}