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@ARTICLE{Joshi:162700,
      author       = {Joshi, Pranav and Riffel, Florian and Satoh, Kanayo and
                      Enomoto, Masahiro and Qamar, Seema and Scheiblich, Hannah
                      and Villacampa, Nàdia and Kumar, Sathish and Theil, Sandra
                      and Parhizkar, Samira and Haass, Christian and Heneka,
                      Michael and Fraser, Paul E and St George-Hyslop, Peter and
                      Walter, Jochen},
      title        = {{D}ifferential interaction with {TREM}2 modulates
                      microglial uptake of modified {A}β species.},
      journal      = {Glia},
      volume       = {69},
      number       = {12},
      issn         = {1098-1136},
      address      = {Bognor Regis [u.a.]},
      publisher    = {Wiley-Liss},
      reportid     = {DZNE-2021-01357},
      pages        = {2917 - 2932},
      year         = {2021},
      abstract     = {Rare coding variants of the microglial triggering receptor
                      expressed on myeloid cells 2 (TREM2) confer an increased
                      risk for Alzheimer's disease (AD) characterized by the
                      progressive accumulation of aggregated forms of amyloid β
                      peptides (Aβ). Aβ peptides are generated by proteolytic
                      processing of the amyloid precursor protein (APP).
                      Heterogeneity in proteolytic cleavages and additional
                      post-translational modifications result in the production of
                      several distinct Aβ variants that could differ in their
                      aggregation behavior and toxic properties. Here, we sought
                      to assess whether post-translational modifications of Aβ
                      affect the interaction with TREM2. Biophysical and
                      biochemical methods revealed that TREM2 preferentially
                      interacts with oligomeric Aβ, and that phosphorylation of
                      Aβ increases this interaction. Phosphorylation of Aβ also
                      affected the TREM2 dependent interaction and phagocytosis by
                      primary microglia and in APP transgenic mouse models. Thus,
                      TREM2 function is important for sensing phosphorylated Aβ
                      variants in distinct aggregation states and reduces the
                      accumulation and deposition of these toxic Aβ species in
                      preclinical models of Alzheimer's disease.},
      keywords     = {Alzheimer Disease: genetics / Alzheimer Disease: metabolism
                      / Amyloid beta-Peptides: metabolism / Amyloid beta-Protein
                      Precursor: genetics / Amyloid beta-Protein Precursor:
                      metabolism / Animals / Disease Models, Animal / Membrane
                      Glycoproteins: genetics / Membrane Glycoproteins: metabolism
                      / Mice / Mice, Transgenic / Microglia: metabolism /
                      Receptors, Immunologic: genetics / Receptors, Immunologic:
                      metabolism / Alzheimer's disease (Other) / FTD mutation
                      (Other) / TREM2 (Other) / amyloid β (Other) /
                      phosphorylation (Other) / post-translational modification
                      (Other)},
      cin          = {Biomarker / AG Heneka / AG Haass / Tech Transfer},
      ddc          = {610},
      cid          = {I:(DE-2719)1011301 / I:(DE-2719)1011303 /
                      I:(DE-2719)1110007 / I:(DE-2719)1030028},
      pnm          = {353 - Clinical and Health Care Research (POF4-353) / 352 -
                      Disease Mechanisms (POF4-352) / 899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-353 / G:(DE-HGF)POF4-352 /
                      G:(DE-HGF)POF4-899},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:34427354},
      doi          = {10.1002/glia.24077},
      url          = {https://pub.dzne.de/record/162700},
}