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@ARTICLE{Liepelt:817934,
      author       = {Liepelt, Anke and Naarmann-de Vries, Isabel S and Simons,
                      Nadine and Eichelbaum, Katrin and Föhr, Sophia and Archer,
                      Stuart K and Castello, Alfredo and Usadel, Björn and
                      Krijgsveld, Jeroen and Preiss, Thomas and Marx, Gernot and
                      Hentze, Matthias W and Ostareck, Dirk H and
                      Ostareck-Lederer, Antje},
      title        = {{I}dentification of {RNA}-binding {P}roteins in
                      {M}acrophages by {I}nteractome {C}apture.},
      journal      = {Molecular $\&$ cellular proteomics},
      volume       = {15},
      number       = {8},
      issn         = {1535-9484},
      address      = {Bethesda, Md.},
      publisher    = {The American Society for Biochemistry and Molecular
                      Biology},
      reportid     = {FZJ-2016-04526},
      pages        = {2699 - 2714},
      year         = {2016},
      abstract     = {Pathogen components, such as lipopolysaccharides of
                      Gram-negative bacteria that activate Toll-like receptor 4,
                      induce mitogen activated protein kinases and NFκB through
                      different downstream pathways to stimulate pro- and
                      anti-inflammatory cytokine expression. Importantly,
                      post-transcriptional control of the expression of Toll-like
                      receptor 4 downstream signaling molecules contributes to the
                      tight regulation of inflammatory cytokine synthesis in
                      macrophages. Emerging evidence highlights the role of
                      RNA-binding proteins (RBPs) in the post-transcriptional
                      control of the innate immune response. To systematically
                      identify macrophage RBPs and their response to LPS
                      stimulation, we employed RNA interactome capture in
                      LPS-induced and untreated murine RAW 264.7 macrophages. This
                      combines RBP-crosslinking to RNA, cell lysis, oligo(dT)
                      capture of polyadenylated RNAs and mass spectrometry
                      analysis of associated proteins. Our data revealed 402
                      proteins of the macrophage RNA interactome including 91
                      previously not annotated as RBPs. A comparison with
                      published RNA interactomes classified 32 RBPs uniquely
                      identified in RAW 264.7 macrophages. Of these, 19 proteins
                      are linked to biochemical activities not directly related to
                      RNA. From this group, we validated the HSP90 cochaperone P23
                      that was demonstrated to exhibit cytosolic prostaglandin E2
                      synthase 3 (PTGES3) activity, and the hematopoietic
                      cell-specific LYN substrate 1 (HCLS1 or HS1), a
                      hematopoietic cell-specific adapter molecule, as novel
                      macrophage RBPs. Our study expands the mammalian RBP
                      repertoire, and identifies macrophage RBPs that respond to
                      LPS. These RBPs are prime candidates for the
                      post-transcriptional regulation and execution of LPS-induced
                      signaling pathways and the innate immune response.
                      Macrophage RBP data have been deposited to ProteomeXchange
                      with identifier PXD002890.},
      cin          = {IBG-2},
      ddc          = {540},
      cid          = {I:(DE-Juel1)IBG-2-20101118},
      pnm          = {582 - Plant Science (POF3-582)},
      pid          = {G:(DE-HGF)POF3-582},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:27281784},
      UT           = {WOS:000380809100012},
      doi          = {10.1074/mcp.M115.056564},
      url          = {https://juser.fz-juelich.de/record/817934},
}