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@ARTICLE{Carrasco:143556,
      author       = {K. Carrasco and A. Boufenzer and L. Jolly and H. Le Cordier
                      and G. Wang and A. J. Heck and A. Cerwenka$^*$ and E. Vinolo
                      and A. Nazabal and A. Kriznik and P. Launay and S. Gibot and
                      M. Derive},
      title        = {{TREM}-1 multimerization is essential for its activation on
                      monocytes and neutrophils.},
      journal      = {Cellular $\&$ molecular immunology},
      volume       = {16},
      number       = {5},
      issn         = {2042-0226},
      address      = {London [u.a.]},
      publisher    = {Nature Publ. Group},
      reportid     = {DKFZ-2019-01137},
      pages        = {460 - 472},
      year         = {2019},
      abstract     = {The triggering receptor expressed on myeloid cells-1
                      (TREM-1) is a receptor expressed on innate immune cells. By
                      promoting the amplification of inflammatory signals that are
                      initially triggered by Toll-like receptors (TLRs), TREM-1
                      has been characterized as a major player in the
                      pathophysiology of acute and chronic inflammatory diseases,
                      such as septic shock, myocardial infarction,
                      atherosclerosis, and inflammatory bowel diseases. However,
                      the molecular events leading to the activation of TREM-1 in
                      innate immune cells remain unknown. Here, we show that
                      TREM-1 is activated by multimerization and that the levels
                      of intracellular Ca2+ release, reactive oxygen species, and
                      cytokine production correlate with the degree of TREM-1
                      aggregation. TREM-1 activation on primary human monocytes by
                      LPS required a two-step process consisting of upregulation
                      followed by clustering of TREM-1 at the cell surface, in
                      contrast to primary human neutrophils, where LPS induced a
                      rapid cell membrane reorganization of TREM-1, which
                      confirmed that TREM-1 is regulated differently in primary
                      human neutrophils and monocytes. In addition, we show that
                      the ectodomain of TREM-1 is able to homooligomerize in a
                      concentration-dependent manner, which suggests that the
                      clustering of TREM-1 on the membrane promotes its
                      oligomerization. We further show that the adapter protein
                      DAP12 stabilizes TREM-1 surface expression and
                      multimerization. TREM-1 multimerization at the cell surface
                      is also mediated by its endogenous ligand, a conclusion
                      supported by the ability of the TREM-1 inhibitor LR12 to
                      limit TREM-1 multimerization. These results provide evidence
                      for ligand-induced, receptor-mediated dimerization of
                      TREM-1. Collectively, our findings uncover the mechanisms
                      necessary for TREM-1 activation in monocytes and
                      neutrophils.},
      cin          = {D080},
      ddc          = {610},
      cid          = {I:(DE-He78)D080-20160331},
      pnm          = {314 - Tumor immunology (POF3-314)},
      pid          = {G:(DE-HGF)POF3-314},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:29568119},
      doi          = {10.1038/s41423-018-0003-5},
      url          = {https://inrepo02.dkfz.de/record/143556},
}