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@ARTICLE{Hering:291762,
      author       = {M. Hering$^*$ and A. A. M. Madi$^*$ and R. Sandhoff$^*$ and
                      S. Ma$^*$ and J. Wu$^*$ and A. Mieg$^*$ and K. Richter$^*$
                      and K. Mohr$^*$ and N. Knabe$^*$ and D. Stichling$^*$ and G.
                      Poschet and F. Bestvater$^*$ and L. J. Frank$^*$ and J.
                      Utikal$^*$ and V. Umansky$^*$ and G. Cui$^*$},
      title        = {{S}phinganine recruits {TLR}4 adaptors in macrophages and
                      promotes inflammation in murine models of sepsis and
                      melanoma.},
      journal      = {Nature Communications},
      volume       = {15},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Nature Publishing Group UK},
      reportid     = {DKFZ-2024-01498},
      pages        = {6067},
      year         = {2024},
      note         = {#EA:D192#EA:A370#LA:D192# / HI-TRON},
      abstract     = {After recognizing its ligand lipopolysaccharide, Toll-like
                      receptor 4 (TLR4) recruits adaptor proteins to the cell
                      membrane, thereby initiating downstream signaling and
                      triggering inflammation. Whether this recruitment of adaptor
                      proteins is dependent solely on protein-protein interactions
                      is unknown. Here, we report that the sphingolipid
                      sphinganine physically interacts with the adaptor proteins
                      MyD88 and TIRAP and promotes MyD88 recruitment in
                      macrophages. Myeloid cell-specific deficiency in serine
                      palmitoyltransferase long chain base subunit 2, which
                      encodes the key enzyme catalyzing sphingolipid biosynthesis,
                      decreases the membrane recruitment of MyD88 and inhibits
                      inflammatory responses in in vitro bone marrow-derived
                      macrophage and in vivo sepsis models. In a melanoma mouse
                      model, serine palmitoyltransferase long chain base subunit 2
                      deficiency decreases anti-tumor myeloid cell responses and
                      increases tumor growth. Therefore, sphinganine biosynthesis
                      is required for the initiation of TLR4 signal transduction
                      and serves as a checkpoint for macrophage pattern
                      recognition in sepsis and melanoma mouse models.},
      keywords     = {Animals / Toll-Like Receptor 4: metabolism / Sepsis:
                      metabolism / Macrophages: metabolism / Myeloid
                      Differentiation Factor 88: metabolism / Mice / Sphingosine:
                      analogs $\&$ derivatives / Sphingosine: metabolism /
                      Melanoma: metabolism / Melanoma: pathology / Melanoma:
                      genetics / Serine C-Palmitoyltransferase: metabolism /
                      Serine C-Palmitoyltransferase: genetics / Humans / Signal
                      Transduction / Disease Models, Animal / Inflammation:
                      metabolism / Receptors, Interleukin-1: metabolism /
                      Receptors, Interleukin-1: genetics / Membrane Glycoproteins:
                      metabolism / Membrane Glycoproteins: genetics / Mice, Inbred
                      C57BL / Mice, Knockout / HEK293 Cells / Lipopolysaccharides
                      / Toll-Like Receptor 4 (NLM Chemicals) / Myeloid
                      Differentiation Factor 88 (NLM Chemicals) / Sphingosine (NLM
                      Chemicals) / Tlr4 protein, mouse (NLM Chemicals) / Serine
                      C-Palmitoyltransferase (NLM Chemicals) / safingol (NLM
                      Chemicals) / Receptors, Interleukin-1 (NLM Chemicals) /
                      Membrane Glycoproteins (NLM Chemicals) / Myd88 protein,
                      mouse (NLM Chemicals) / TIRAP protein, mouse (NLM Chemicals)
                      / TIRAP protein, human (NLM Chemicals) / Lipopolysaccharides
                      (NLM Chemicals)},
      cin          = {D192 / A370 / A411 / W230 / W210 / D110},
      ddc          = {500},
      cid          = {I:(DE-He78)D192-20160331 / I:(DE-He78)A370-20160331 /
                      I:(DE-He78)A411-20160331 / I:(DE-He78)W230-20160331 /
                      I:(DE-He78)W210-20160331 / I:(DE-He78)D110-20160331},
      pnm          = {314 - Immunologie und Krebs (POF4-314)},
      pid          = {G:(DE-HGF)POF4-314},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39025856},
      pmc          = {pmc:PMC11258287},
      doi          = {10.1038/s41467-024-50341-w},
      url          = {https://inrepo02.dkfz.de/record/291762},
}