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@ARTICLE{Papadopoulou:140605,
      author       = {Papadopoulou, Alkmini A and Müller, Stephan A and Mentrup,
                      Torben and Shmueli, Merav D and Niemeyer, Johannes and
                      Haug-Kröper, Martina and von Blume, Julia and Mayerhofer,
                      Artur and Feederle, Regina and Schröder, Bernd and
                      Lichtenthaler, Stefan F and Fluhrer, Regina},
      title        = {{S}ignal {P}eptide {P}eptidase-{L}ike 2c ({SPPL}2c) impairs
                      vesicular transport and cleaves {SNARE} proteins.},
      journal      = {EMBO reports},
      volume       = {20},
      number       = {3},
      issn         = {1469-221X},
      address      = {Hoboken, NJ [u.a.]},
      publisher    = {Wiley},
      reportid     = {DZNE-2020-06927},
      pages        = {e46451},
      year         = {2019},
      note         = {Title corrected according to Corrigendum: EMBO rep (2019)
                      20: e48133 https://doi.org/10.15252/embr.201948133},
      abstract     = {Members of the GxGD-type intramembrane aspartyl proteases
                      have emerged as key players not only in fundamental cellular
                      processes such as B-cell development or protein
                      glycosylation, but also in development of pathologies, such
                      as Alzheimer's disease or hepatitis virus infections.
                      However, one member of this protease family, signal peptide
                      peptidase-like 2c (SPPL2c), remains orphan and its
                      capability of proteolysis as well as its physiological
                      function is still enigmatic. Here, we demonstrate that
                      SPPL2c is catalytically active and identify a variety of
                      SPPL2c candidate substrates using proteomics. The majority
                      of the SPPL2c candidate substrates cluster to the biological
                      process of vesicular trafficking. Analysis of selected SNARE
                      proteins reveals proteolytic processing by SPPL2c that
                      impairs vesicular transport and causes retention of cargo
                      proteins in the endoplasmic reticulum. As a consequence, the
                      integrity of subcellular compartments, in particular the
                      Golgi, is disturbed. Together with a strikingly high
                      physiological SPPL2c expression in testis, our data suggest
                      involvement of SPPL2c in acrosome formation during
                      spermatogenesis.},
      cin          = {AG Haass / AG Lichtenthaler / AG Feederle / AG Fluhrer},
      ddc          = {570},
      cid          = {I:(DE-2719)1110007 / I:(DE-2719)1110006 /
                      I:(DE-2719)1140004 / I:(DE-2719)1110000-2},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:30733281},
      pmc          = {pmc:PMC6399617},
      doi          = {10.15252/embr.201846451},
      url          = {https://pub.dzne.de/record/140605},
}