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@ARTICLE{Gollowitzer:299480,
      author       = {A. Gollowitzer and H. Pein and Z. Rao and L. Waltl and L.
                      Bereuter and K. Loeser and T. Meyer and V. Jafari and F.
                      Witt and R. Winkler and F. Su and S. Große and M. Thürmer
                      and J. Grander and M. Hotze and S. Harder and L. Espada and
                      A. Magnutzki and R. Gstir and C. Weinigel and S. Rummler and
                      G. Bonn and J. Pachmayr and M. Ermolaeva and T. Harayama and
                      H. Schlüter and C. Kosan and R. Heller and K. Thedieck$^*$
                      and M. Schmitt and T. Shimizu and J. Popp and H. Shindou and
                      M. Kwiatkowski and A. Koeberle},
      title        = {{A}ttenuated growth factor signaling during cell death
                      initiation sensitizes membranes towards peroxidation.},
      journal      = {Nature Communications},
      volume       = {16},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {DKFZ-2025-00440},
      pages        = {1774},
      year         = {2025},
      abstract     = {Cell death programs such as apoptosis and ferroptosis are
                      associated with aberrant redox homeostasis linked to lipid
                      metabolism and membrane function. Evidence for cross-talk
                      between these programs is emerging. Here, we show that
                      cytotoxic stress channels polyunsaturated fatty acids via
                      lysophospholipid acyltransferase 12 into phospholipids that
                      become susceptible to peroxidation under additional redox
                      stress. This reprogramming is associated with altered
                      acyl-CoA synthetase isoenzyme expression and caused by a
                      decrease in growth factor receptor tyrosine kinase
                      (RTK)-phosphatidylinositol-3-kinase signaling, resulting in
                      suppressed fatty acid biosynthesis, for specific stressors
                      via impaired Akt-SREBP1 activation. The reduced availability
                      of de novo synthesized fatty acids favors the channeling of
                      polyunsaturated fatty acids into phospholipids. Growth
                      factor withdrawal by serum starvation mimics this phenotype,
                      whereas RTK ligands counteract it. We conclude that
                      attenuated RTK signaling during cell death initiation
                      increases cells' susceptibility to oxidative membrane damage
                      at the interface of apoptosis and alternative cell death
                      programs.},
      keywords     = {Signal Transduction / Humans / Lipid Peroxidation /
                      Apoptosis / Cell Membrane: metabolism / Sterol Regulatory
                      Element Binding Protein 1: metabolism / Sterol Regulatory
                      Element Binding Protein 1: genetics / Proto-Oncogene
                      Proteins c-akt: metabolism / Phospholipids: metabolism /
                      Fatty Acids, Unsaturated: metabolism / Cell Death / Coenzyme
                      A Ligases: metabolism / Coenzyme A Ligases: genetics /
                      Animals / Phosphatidylinositol 3-Kinases: metabolism /
                      Oxidation-Reduction / Oxidative Stress / Ferroptosis /
                      Sterol Regulatory Element Binding Protein 1 (NLM Chemicals)
                      / Proto-Oncogene Proteins c-akt (NLM Chemicals) /
                      Phospholipids (NLM Chemicals) / Fatty Acids, Unsaturated
                      (NLM Chemicals) / Coenzyme A Ligases (NLM Chemicals) /
                      SREBF1 protein, human (NLM Chemicals) / Phosphatidylinositol
                      3-Kinases (NLM Chemicals)},
      cin          = {ED01},
      ddc          = {500},
      cid          = {I:(DE-He78)ED01-20160331},
      pnm          = {899 - ohne Topic (POF4-899)},
      pid          = {G:(DE-HGF)POF4-899},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40000627},
      doi          = {10.1038/s41467-025-56711-2},
      url          = {https://inrepo02.dkfz.de/record/299480},
}