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@ARTICLE{Mentrup:139528,
      author       = {Mentrup, Torben and Fluhrer, Regina and Schröder, Bernd},
      title        = {{L}atest emerging functions of {SPP}/{SPPL} intramembrane
                      proteases.},
      journal      = {European journal of cell biology},
      volume       = {96},
      number       = {5},
      issn         = {0171-9335},
      address      = {Amsterdam},
      publisher    = {Elsevier74814},
      reportid     = {DZNE-2020-05850},
      pages        = {372-382},
      year         = {2017},
      abstract     = {Signal peptide peptidase (SPP) and the four related
                      SPP-like (SPPL) proteases are homologues of the presenilins,
                      which comprise the catalytic centre of the γ-secretase
                      complex. SPP/SPPL proteases are GxGD-type aspartyl
                      intramembrane proteases selective for substrates with a type
                      II membrane topology. Subcellular localisations of SPP/SPPL
                      proteases range from the early secretory pathway to the
                      plasma membrane and the endocytic system. Similarly diverse
                      are their functional roles at the cellular level covering
                      the turnover of signal peptides and membrane proteins, a
                      contribution to the ERAD pathway as well as the regulation
                      of cellular protein glycosylation and certain signaling
                      pathways. Much less well understood are the physiological
                      functions of SPP/SPPL proteases in complex organisms.
                      Whereas a major role of SPPL2a for homeostasis of B cells
                      and dendritic cells has been documented in mice, in vivo
                      functions of SPP and the other SPPLs remain largely elusive
                      to date. SPP/SPPL proteases contribute to regulated
                      intramembrane proteolysis (RIP), a sequential processing of
                      single-spanning transmembrane proteins by an ectodomain
                      sheddase and an intramembrane-cleaving protease (I-CLIP).
                      However, recent studies reported the cleavage of
                      tail-anchored and multi-pass membrane proteins by SPP as
                      well as the capability of SPPL3 to accept substrates without
                      a preceding ectodomain shedding. This revealed that the
                      mechanistic properties within this family are more diverse
                      than initially thought. With this review, we aim to provide
                      an update on recent achievements in defining the function
                      and (patho-) physiological relevance of SPP/SPPL proteases
                      and to highlight open questions in the field.},
      subtyp        = {Review Article},
      keywords     = {Animals / Aspartic Acid Endopeptidases / Humans / Membrane
                      Proteins / Membrane Proteins (NLM Chemicals) / Aspartic Acid
                      Endopeptidases (NLM Chemicals) / signal peptide peptidase
                      (NLM Chemicals)},
      cin          = {AG Fluhrer},
      ddc          = {570},
      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:28366434},
      doi          = {10.1016/j.ejcb.2017.03.002},
      url          = {https://pub.dzne.de/record/139528},
}