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@ARTICLE{Koo:153465,
      author       = {Koo, Chek Ziu and Harrison, Neale and Noy, Peter J. and
                      Szyroka, Justyna and Matthews, Alexandra L. and Hsia,
                      Hung-En and Müller, Stephan A and Tüshaus, Johanna and
                      Goulding, Joelle and Willis, Katie and Apicella, Clara and
                      Cragoe, Bethany and Davis, Edward and Keles, Murat and
                      Malinova, Antonia and McFarlane, Thomas A. and Morrison,
                      Philip R. and Nguyen, Hanh T. H. and Sykes, Michael C. and
                      Ahmed, Haroon and Di Maio, Alessandro and Seipold, Lisa and
                      Saftig, Paul and Cull, Eleanor and Pliotas, Christos and
                      Rubinstein, Eric and Poulter, Natalie S. and Briddon,
                      Stephen J. and Holliday, Nicholas D. and Lichtenthaler,
                      Stefan and Tomlinson, Michael G.},
      title        = {{T}he tetraspanin {T}span15 is an essential subunit of an
                      {ADAM}10 scissor complex},
      journal      = {The journal of biological chemistry},
      volume       = {295},
      number       = {36},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {DZNE-2020-01462},
      pages        = {12822 - 12839},
      year         = {2020},
      abstract     = {A disintegrin and metalloprotease 10 (ADAM10) is a
                      transmembrane protein essential for embryonic development,
                      and its dysregulation underlies disorders such as cancer,
                      Alzheimer's disease, and inflammation. ADAM10 is a
                      "molecular scissor" that proteolytically cleaves the
                      extracellular region from >100 substrates, including Notch,
                      amyloid precursor protein, cadherins, growth factors, and
                      chemokines. ADAM10 has been recently proposed to function as
                      six distinct scissors with different substrates, depending
                      on its association with one of six regulatory tetraspanins,
                      termed TspanC8s. However, it remains unclear to what degree
                      ADAM10 function critically depends on a TspanC8 partner, and
                      a lack of monoclonal antibodies specific for most TspanC8s
                      has hindered investigation of this question. To address this
                      knowledge gap, here we designed an immunogen to generate the
                      first monoclonal antibodies targeting Tspan15, a model
                      TspanC8. The immunogen was created in an ADAM10-knockout
                      mouse cell line stably overexpressing human Tspan15, because
                      we hypothesized that expression in this cell line would
                      expose epitopes that are normally blocked by ADAM10.
                      Following immunization of mice, this immunogen strategy
                      generated four Tspan15 antibodies. Using these antibodies,
                      we show that endogenous Tspan15 and ADAM10 co-localize on
                      the cell surface, that ADAM10 is the principal
                      Tspan15-interacting protein, that endogenous Tspan15
                      expression requires ADAM10 in cell lines and primary cells,
                      and that a synthetic ADAM10/Tspan15 fusion protein is a
                      functional scissor. Furthermore, two of the four antibodies
                      impaired ADAM10/Tspan15 activity. These findings suggest
                      that Tspan15 directly interacts with ADAM10 in a functional
                      scissor complex.},
      keywords     = {A549 Cells / ADAM10 Protein: genetics / ADAM10 Protein:
                      metabolism / Amyloid Precursor Protein Secretases: genetics
                      / Amyloid Precursor Protein Secretases: metabolism / Animals
                      / HEK293 Cells / Humans / Jurkat Cells / Membrane Proteins:
                      genetics / Membrane Proteins: metabolism / Mice / Mice,
                      Knockout / Multiprotein Complexes: genetics / Multiprotein
                      Complexes: metabolism / Tetraspanins: genetics /
                      Tetraspanins: metabolism},
      cin          = {AG Lichtenthaler},
      ddc          = {540},
      cid          = {I:(DE-2719)1110006},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pmc          = {pmc:PMC7476718},
      pubmed       = {pmid:32111735},
      doi          = {10.1074/jbc.RA120.012601},
      url          = {https://pub.dzne.de/record/153465},
}