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@ARTICLE{Jules:139338,
      author       = {Jules, Felix and Sauvageau, Etienne and Dumaresq-Doiron,
                      Karine and Mazzaferri, Javier and Haug-Kröper, Martina and
                      Fluhrer, Regina and Costantino, Santiago and Lefrancois,
                      Stephane},
      title        = {{CLN}5 is cleaved by members of the {SPP}/{SPPL} family to
                      produce a mature soluble protein.},
      journal      = {Experimental cell research},
      volume       = {357},
      number       = {1},
      issn         = {0014-4827},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {DZNE-2020-05660},
      pages        = {40-50},
      year         = {2017},
      abstract     = {The Neuronal ceroid lipofuscinoses (NCLs) are a group of
                      recessive disorders of childhood with overlapping symptoms
                      including vision loss, ataxia, cognitive regression and
                      premature death. 14 different genes have been linked to NCLs
                      (CLN1-CLN14), but the functions of the proteins encoded by
                      the majority of these genes have not been fully elucidated.
                      Mutations in the CLN5 gene are responsible for the Finnish
                      variant late-infantile form of NCL (Finnish vLINCL). CLN5 is
                      translated as a 407 amino acid transmembrane domain
                      containing protein that is heavily glycosylated, and
                      subsequently cleaved into a mature soluble protein.
                      Functionally, CLN5 is implicated in the recruitment of the
                      retromer complex to endosomes, which is required to sort the
                      lysosomal sorting receptors from endosomes to the
                      trans-Golgi network. The mechanism that processes CLN5 into
                      a mature soluble protein is currently not known. Herein, we
                      demonstrate that CLN5 is initially translated as a type II
                      transmembrane protein and subsequently cleaved by SPPL3, a
                      member of the SPP/SPPL intramembrane protease family, into a
                      mature soluble protein consisting of residues 93-407. The
                      remaining N-terminal fragment is then cleaved by SPPL3 and
                      SPPL2b and degraded in the proteasome. This work further
                      characterizes the biology of CLN5 in the hopes of
                      identifying a novel therapeutic strategy for affected
                      children.},
      keywords     = {Lysosome-Associated Membrane Glycoproteins / Aspartic Acid
                      Endopeptidases: metabolism / Cell Line / Endosomes:
                      metabolism / Humans / Lysosomes: metabolism / Membrane
                      Proteins: metabolism / Neuronal Ceroid-Lipofuscinoses:
                      metabolism / Protein Transport / Solubility / trans-Golgi
                      Network: metabolism / CLN5 protein, human (NLM Chemicals) /
                      Membrane Proteins (NLM Chemicals) / Aspartic Acid
                      Endopeptidases (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:28442266},
      doi          = {10.1016/j.yexcr.2017.04.024},
      url          = {https://pub.dzne.de/record/139338},
}