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@ARTICLE{Cuartero:136624,
      author       = {Cuartero, Yasmina and Mellado, Maravillas and Capell, Anja
                      and Alvarez-Dolado, Manuel and Verges, Marcel},
      title        = {{R}etromer regulates postendocytic sorting of β-secretase
                      in polarized {M}adin-{D}arby canine kidney cells.},
      journal      = {Traffic},
      volume       = {13},
      number       = {10},
      issn         = {1398-9219},
      address      = {Oxford},
      publisher    = {Wiley-Blackwell},
      reportid     = {DZNE-2020-02946},
      pages        = {1393-1410},
      year         = {2012},
      abstract     = {β-Amyloid (Aβ) peptides are generated from the successive
                      proteolytic processing of the amyloid precursor protein
                      (APP) by the β-APP cleaving enzyme (BACE or β-secretase)
                      and the γ-secretase complex. Initial cleavage of APP by
                      BACE leads into the amyloidogenic pathway, causing or
                      exacerbating Alzheimer's disease. Therefore, their
                      intracellular traffic can determine how easily and
                      frequently BACE has access to and cleaves APP. Here, we have
                      used polarized Madin-Darby canine kidney (MDCK) cells stably
                      expressing APP and BACE to examine the regulation of their
                      polarized trafficking by retromer, a protein complex
                      previously implicated in their endosome-to-Golgi transport.
                      Our data show that retromer interacts with BACE and
                      regulates its postendocytic sorting in polarized MDCK cells.
                      Depleting retromer, inhibiting retromer function, or
                      preventing BACE interaction with retromer, alters
                      trafficking of BACE, which thereby increases its
                      localization in the early endocytic compartment. As a
                      result, this slows endocytosis of apically localized BACE,
                      promoting its recycling and apical-to-basolateral
                      transcytosis, which increases APP/BACE interaction and
                      subsequent cleavage of APP toward generation and secretion
                      of Aβ peptides.},
      keywords     = {Amyloid Precursor Protein Secretases: chemistry / Amyloid
                      Precursor Protein Secretases: genetics / Amyloid Precursor
                      Protein Secretases: metabolism / Amyloid beta-Protein
                      Precursor: metabolism / Animals / Cell Line / Dogs /
                      Endocytosis / Endosomes: metabolism / Golgi Apparatus:
                      metabolism / Madin Darby Canine Kidney Cells / Mice /
                      Multiprotein Complexes: metabolism / Mutation / Protein
                      Interaction Domains and Motifs / Protein Transport /
                      Vesicular Transport Proteins: metabolism / Amyloid
                      beta-Protein Precursor (NLM Chemicals) / Multiprotein
                      Complexes (NLM Chemicals) / Vesicular Transport Proteins
                      (NLM Chemicals) / Amyloid Precursor Protein Secretases (NLM
                      Chemicals)},
      cin          = {Ext LMU},
      ddc          = {570},
      cid          = {I:(DE-2719)5000048},
      pnm          = {342 - Disease Mechanisms and Model Systems (POF3-342)},
      pid          = {G:(DE-HGF)POF3-342},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:22758778},
      doi          = {10.1111/j.1600-0854.2012.01392.x},
      url          = {https://pub.dzne.de/record/136624},
}