% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Chen:294550,
      author       = {Z. Chen and A. Inague and K. Kaushal$^*$ and G. Fazeli and
                      D. Schilling$^*$ and T. N. Xavier da Silva and A. F. Dos
                      Santos and T. Cheytan$^*$ and F. P. Freitas and U. Yildiz
                      and L. G. Viviani and R. S. Lima and M. P. Pinz and I.
                      Medeiros and T. S. Iijima and T. G. P. Alegria and R.
                      Pereira da Silva and L. R. Diniz and S. Weinzweig and J.
                      Klein-Seetharaman and A. Trumpp$^*$ and A. Mañas and R.
                      Hondal and C. Bartenhagen and M. Fischer and B. K. Shimada
                      and L. A. Seale and T. S. Chillon and M. Fabiano and L.
                      Schomburg and U. Schweizer and L. E. Netto and F. C. Meotti
                      and T. P. Dick$^*$ and H. Alborzinia$^*$ and S. Miyamoto and
                      J. P. Friedmann Angeli},
      title        = {{PRDX}6 contributes to selenocysteine metabolism and
                      ferroptosis resistance.},
      journal      = {Molecular cell},
      volume       = {84},
      number       = {23},
      issn         = {1097-2765},
      address      = {New York, NY},
      publisher    = {Elsevier},
      reportid     = {DKFZ-2024-02325},
      pages        = {4645–4659.e9},
      year         = {2024},
      note         = {DKFZ-ZMBH Alliance / 84(23), pp. 4645–4659.e9},
      abstract     = {Selenocysteine (Sec) metabolism is crucial for cellular
                      function and ferroptosis prevention and begins with the
                      uptake of the Sec carrier, selenoprotein P (SELENOP).
                      Following uptake, Sec released from SELENOP is metabolized
                      via selenocysteine lyase (SCLY), producing selenide, a
                      substrate for selenophosphate synthetase 2 (SEPHS2), which
                      provides the essential selenium donor, selenophosphate
                      (H2SePO3-), for the biosynthesis of the Sec-tRNA. Here, we
                      discovered an alternative pathway in Sec metabolism mediated
                      by peroxiredoxin 6 (PRDX6), independent of SCLY.
                      Mechanistically, we demonstrate that PRDX6 can readily react
                      with selenide and interact with SEPHS2, potentially acting
                      as a selenium delivery system. Moreover, we demonstrate the
                      functional significance of this alternative route in human
                      cancer cells, revealing a notable association between
                      elevated expression of PRDX6 and human MYCN-amplified
                      neuroblastoma subtype. Our study sheds light on a previously
                      unrecognized aspect of Sec metabolism and its implications
                      in ferroptosis, offering further possibilities for
                      therapeutic exploitation.},
      keywords     = {cancer metabolism (Other) / cell death (Other) /
                      ferroptosis (Other) / neuroblastoma (Other) / selenium
                      (Other) / selenocysteine metabolism (Other)},
      cin          = {A010 / A160},
      ddc          = {610},
      cid          = {I:(DE-He78)A010-20160331 / I:(DE-He78)A160-20160331},
      pnm          = {311 - Zellbiologie und Tumorbiologie (POF4-311)},
      pid          = {G:(DE-HGF)POF4-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:39547224},
      doi          = {10.1016/j.molcel.2024.10.027},
      url          = {https://inrepo02.dkfz.de/record/294550},
}