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@ARTICLE{Fleck:136892,
      author       = {Fleck, Daniel and van Bebber, Frauke and Colombo, Alessio
                      and Galante, Chiara and Schwenk, Benjamin M and Rabe, Linnea
                      and Hampel, Heike and Novak, Bozidar and Kremmer, Elisabeth
                      and Tahirovic, Sabina and Edbauer, Dieter and Lichtenthaler,
                      Stefan F and Schmid, Bettina and Willem, Michael and Haass,
                      Christian},
      title        = {{D}ual cleavage of neuregulin 1 type {III} by {BACE}1 and
                      {ADAM}17 liberates its {EGF}-like domain and allows
                      paracrine signaling.},
      journal      = {The journal of neuroscience},
      volume       = {33},
      number       = {18},
      issn         = {0270-6474},
      address      = {Washington, DC},
      publisher    = {Soc.57413},
      reportid     = {DZNE-2020-03214},
      pages        = {7856-7869},
      year         = {2013},
      abstract     = {Proteolytic shedding of cell surface proteins generates
                      paracrine signals involved in numerous signaling pathways.
                      Neuregulin 1 (NRG1) type III is involved in myelination of
                      the peripheral nervous system, for which it requires
                      proteolytic activation by proteases of the ADAM family and
                      BACE1. These proteases are major therapeutic targets for the
                      prevention of Alzheimer's disease because they are also
                      involved in the proteolytic generation of the neurotoxic
                      amyloid β-peptide. Identification and functional
                      investigation of their physiological substrates is therefore
                      of greatest importance in preventing unwanted side effects.
                      Here we investigated proteolytic processing of NRG1 type III
                      and demonstrate that the ectodomain can be cleaved by three
                      different sheddases, namely ADAM10, ADAM17, and BACE1.
                      Surprisingly, we not only found cleavage by ADAM10, ADAM17,
                      and BACE1 C-terminal to the epidermal growth factor
                      (EGF)-like domain, which is believed to play a pivotal role
                      in signaling, but also additional cleavage sites for ADAM17
                      and BACE1 N-terminal to that domain. Proteolytic processing
                      at N- and C-terminal sites of the EGF-like domain results in
                      the secretion of this domain from NRG1 type III. The soluble
                      EGF-like domain is functionally active and stimulates ErbB3
                      signaling in tissue culture assays. Moreover, the soluble
                      EGF-like domain is capable of rescuing hypomyelination in a
                      zebrafish mutant lacking BACE1. Our data suggest that NRG1
                      type III-dependent myelination is not only controlled by
                      membrane-retained NRG1 type III, but also in a paracrine
                      manner via proteolytic liberation of the EGF-like domain.},
      keywords     = {ADAM Proteins: metabolism / ADAM17 Protein / Amyloid
                      Precursor Protein Secretases: metabolism / Animals /
                      Aspartic Acid Endopeptidases: metabolism / Cell Membrane:
                      metabolism / Cells, Cultured / Cricetinae / Cricetulus /
                      Embryo, Mammalian / Epidermal Growth Factor: analogs $\&$
                      derivatives / Epidermal Growth Factor: chemistry / Humans /
                      Immunoprecipitation / Neuregulins: genetics / Neuregulins:
                      metabolism / Neurons / Paracrine Communication: physiology /
                      Phosphorylation / Proteolysis / RNA, Messenger:
                      administration $\&$ dosage / RNA, Messenger: metabolism /
                      RNA, Small Interfering: metabolism / Rats / Rats,
                      Sprague-Dawley / Schwann Cells / Transfection / Zebrafish /
                      NRG3 protein, human (NLM Chemicals) / Neuregulins (NLM
                      Chemicals) / RNA, Messenger (NLM Chemicals) / RNA, Small
                      Interfering (NLM Chemicals) / Epidermal Growth Factor (NLM
                      Chemicals) / Amyloid Precursor Protein Secretases (NLM
                      Chemicals) / Aspartic Acid Endopeptidases (NLM Chemicals) /
                      BACE1 protein, human (NLM Chemicals) / ADAM Proteins (NLM
                      Chemicals) / ADAM17 Protein (NLM Chemicals) / ADAM17
                      protein, human (NLM Chemicals) / Adam17 protein, rat (NLM
                      Chemicals)},
      cin          = {Zebrafish Models ; AG Schmid ; AG Schmid München / AG
                      Lichtenthaler / AG Edbauer / AG Tahirovic / AG Haass old},
      ddc          = {610},
      cid          = {I:(DE-2719)1140002 / I:(DE-2719)1110006 /
                      I:(DE-2719)1110004 / I:(DE-2719)1140003 /
                      I:(DE-2719)1110007},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:23637177},
      pmc          = {pmc:PMC6618983},
      doi          = {10.1523/JNEUROSCI.3372-12.2013},
      url          = {https://pub.dzne.de/record/136892},
}