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@ARTICLE{Obacz:290039,
      author       = {J. Obacz and J. Archambeau and E. Lafont and M. Nivet and
                      S. Martin and M. Aubry and K. Voutetakis and R. Pineau and
                      R. Boniface and D. Sicari and D. Pelizzari-Raymundo and G.
                      Ghukasyan and E. McGrath and E.-I. Vlachavas$^*$ and M. Le
                      Gallo and P. J. Le Reste and K. Barroso and T. Fainsod-Levi
                      and A. Obiedat and Z. Granot and B. Tirosh and J. Samal and
                      A. Pandit and L. Négroni and N. Soriano and A. Monnier and
                      J. Mosser and A. Chatziioannou$^*$ and V. Quillien and E.
                      Chevet and T. Avril},
      title        = {{IRE}1 endoribonuclease signaling promotes myeloid cell
                      infiltration in glioblastoma.},
      journal      = {Neuro-Oncology},
      volume       = {26},
      number       = {5},
      issn         = {1522-8517},
      address      = {Oxford},
      publisher    = {Oxford Univ. Press},
      reportid     = {DKFZ-2024-00944},
      pages        = {858 - 871},
      year         = {2024},
      abstract     = {Intrinsic or environmental stresses trigger the
                      accumulation of improperly folded proteins in the
                      endoplasmic reticulum (ER), leading to ER stress. To cope
                      with this, cells have evolved an adaptive mechanism named
                      the unfolded protein response (UPR) which is hijacked by
                      tumor cells to develop malignant features. Glioblastoma
                      (GB), the most aggressive and lethal primary brain tumor,
                      relies on UPR to sustain growth. We recently showed that
                      IRE1 alpha (referred to IRE1 hereafter), 1 of the UPR
                      transducers, promotes GB invasion, angiogenesis, and
                      infiltration by macrophage. Hence, high tumor IRE1 activity
                      in tumor cells predicts a worse outcome. Herein, we
                      characterized the IRE1-dependent signaling that shapes the
                      immune microenvironment toward monocytes/macrophages and
                      neutrophils.We used human and mouse cellular models in which
                      IRE1 was genetically or pharmacologically invalidated and
                      which were tested in vivo. Publicly available datasets from
                      GB patients were also analyzed to confirm our findings.We
                      showed that IRE1 signaling, through both the transcription
                      factor XBP1s and the regulated IRE1-dependent decay controls
                      the expression of the ubiquitin-conjugating E2 enzyme
                      UBE2D3. In turn, UBE2D3 activates the NFκB pathway,
                      resulting in chemokine production and myeloid infiltration
                      in tumors.Our work identifies a novel IRE1/UBE2D3
                      proinflammatory axis that plays an instrumental role in GB
                      immune regulation.},
      keywords     = {Glioblastoma: pathology / Glioblastoma: metabolism / Humans
                      / Mice / Endoribonucleases: metabolism / Endoribonucleases:
                      genetics / Animals / Protein Serine-Threonine Kinases:
                      metabolism / Protein Serine-Threonine Kinases: genetics /
                      Signal Transduction / Brain Neoplasms: pathology / Brain
                      Neoplasms: metabolism / Myeloid Cells: metabolism / Myeloid
                      Cells: pathology / Unfolded Protein Response / Tumor
                      Microenvironment / Tumor Cells, Cultured / Endoplasmic
                      Reticulum Stress / ER stress (Other) / IRE1 (Other) /
                      chemokines (Other) / glioblastoma (Other) / inflammation
                      (Other) / Endoribonucleases (NLM Chemicals) / Protein
                      Serine-Threonine Kinases (NLM Chemicals) / ERN1 protein,
                      human (NLM Chemicals)},
      cin          = {B050},
      ddc          = {610},
      cid          = {I:(DE-He78)B050-20160331},
      pnm          = {312 - Funktionelle und strukturelle Genomforschung
                      (POF4-312)},
      pid          = {G:(DE-HGF)POF4-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38153426},
      pmc          = {pmc:PMC11066906},
      doi          = {10.1093/neuonc/noad256},
      url          = {https://inrepo02.dkfz.de/record/290039},
}