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@ARTICLE{Mentrup:151555,
      author       = {Mentrup, Torben and Cabrera-Cabrera, Florencia and Fluhrer,
                      Regina and Schröder, Bernd},
      title        = {{P}hysiological functions of {SPP}/{SPPL} intramembrane
                      proteases},
      journal      = {Cellular and molecular life sciences},
      volume       = {77},
      number       = {15},
      issn         = {1420-682X},
      address      = {Cham (ZG)},
      publisher    = {Springer International Publishing AG},
      reportid     = {DZNE-2020-01139},
      pages        = {2959-2979},
      year         = {2020},
      abstract     = {Intramembrane proteolysis describes the cleavage of
                      substrate proteins within their hydrophobic transmembrane
                      segments. Several families of intramembrane proteases have
                      been identified including the aspartyl proteases Signal
                      peptide peptidase (SPP) and its homologues, the SPP-like
                      (SPPL) proteases SPPL2a, SPPL2b, SPPL2c and SPPL3. As
                      presenilin homologues, they employ a similar catalytic
                      mechanism as the well-studied γ-secretase. However,
                      SPP/SPPL proteases cleave transmembrane proteins with a type
                      II topology. The characterisation of SPP/SPPL-deficient
                      mouse models has highlighted a still growing spectrum of
                      biological functions and also promoted the substrate
                      discovery of these proteases. In this review, we will
                      summarise the current hypotheses how phenotypes of these
                      mouse models are linked to the molecular function of the
                      enzymes. At the cellular level, SPP/SPPL-mediated cleavage
                      events rather provide specific regulatory switches than
                      unspecific bulk proteolysis. By this means, a plethora of
                      different cell biological pathways is influenced including
                      signal transduction, membrane trafficking and protein
                      glycosylation.},
      keywords     = {Amyloid Precursor Protein Secretases: metabolism / Animals
                      / Aspartic Acid Endopeptidases: chemistry / Aspartic Acid
                      Endopeptidases: metabolism / Humans / Membrane Proteins:
                      metabolism / Protein Transport / Proteolysis / Signal
                      Transduction / Substrate Specificity},
      cin          = {AG Fluhrer},
      ddc          = {610},
      cid          = {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:32052089},
      pmc          = {pmc:PMC7366577},
      doi          = {10.1007/s00018-020-03470-6},
      url          = {https://pub.dzne.de/record/151555},
}