@article{MayerSchauenburgThompsonSteckeletal.2016,
  author    = {Mayer, Magnus C. and Schauenburg, Linda and Thompson-Steckel, Greta and Dunsing, Valentin and Kaden, Daniela and Voigt, Philipp and Schaefer, Michael and Chiantia, Salvatore and Kennedy, Timothy E. and Multhaup, Gerhard},
  title     = {Amyloid precursor-like protein 1 (APLP1) exhibits stronger zinc-dependent neuronal adhesion than amyloid precursor protein and APLP2},
  series = {Journal of neurochemistry},
  volume    = {137},
  journal   = {Journal of neurochemistry},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {0022-3042},
  doi       = {10.1111/jnc.13540},
  pages     = {266 -- 276},
  year      = {2016},
  abstract  = {The amyloid precursor protein (APP) and its paralogs, amyloid precursor-like protein 1 (APLP1) and APLP2, are metalloproteins with a putative role both in synaptogenesis and in maintaining synapse structure. Here, we studied the effect of zinc on membrane localization, adhesion, and secretase cleavage of APP, APLP1, and APLP2 in cell culture and rat neurons. For this, we employed live-cell microscopy techniques, a microcontact printing adhesion assay and ELISA for protein detection in cell culture supernatants. We report that zinc induces the multimerization of proteins of the amyloid precursor protein family and enriches them at cellular adhesion sites. Thus, zinc facilitates the formation of de novo APP and APLP1 containing adhesion complexes, whereas it does not have such influence on APLP2. Furthermore, zinc-binding prevented cleavage of APP and APLPs by extracellular secretases. In conclusion, the complexation of zinc modulates neuronal functions of APP and APLPs by (i) regulating formation of adhesion complexes, most prominently for APLP1, and (ii) by reducing the concentrations of neurotrophic soluble APP/APLP ectodomains.},
  language  = {en}
}