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@ARTICLE{HnleKreidler:182682,
      author       = {S. Hänle-Kreidler$^*$ and K. Richter$^*$ and I.
                      Hoffmann$^*$},
      title        = {{T}he {SCF}-{FBXW}7 {E}3 ubiquitin ligase triggers
                      degradation of {H}istone 3 {L}ysine 4 methyltransferase
                      complex component {WDR}5 to prevent mitotic slippage.},
      journal      = {The journal of biological chemistry},
      volume       = {298},
      number       = {12},
      issn         = {0021-9258},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {DKFZ-2022-02850},
      pages        = {102703},
      year         = {2022},
      note         = {ISSN 0021-9258 / #EA:F045#LA:F045#},
      abstract     = {During prolonged mitotic arrest induced by anti-microtubule
                      drugs, cell fate decision is determined by two alternative
                      pathways, one leading to cell death, the other inducing
                      premature escape from mitosis by mitotic slippage. FBWX7, a
                      member of the F-box family of proteins and
                      substrate-targeting subunit of the SCF (SKP1-CUL1-F-Box) E3
                      ubiquitin ligase complex promotes mitotic cell death and
                      prevents mitotic slippage, but molecular details underlying
                      these roles for FBWX7 are unclear. In this study, we report
                      that WDR5, a component of the mixed lineage leukemia (MLL)
                      complex of Histone 3 Lysine 4 (H3K4) methyltransferases, is
                      a substrate of FBXW7. We determined by
                      co-immunoprecipitation experiments and in vitro binding
                      assays that WDR5 interacts with FBXW7 in vivo and in vitro.
                      SCF-FBXW7 mediates ubiquitination of WDR5 and targets it for
                      proteasomal degradation. Furthermore, we find that WDR5
                      depletion counteracts FBXW7 loss-of-function by reducing
                      mitotic slippage and polyploidization. In conclusion, our
                      data elucidate a new mechanism in mitotic cell fate
                      regulation which might contribute to prevent chemotherapy
                      resistance in patients after anti-microtubule drug
                      treatment.},
      keywords     = {FBXW7 (Other) / WDR5 (Other) / chemoresistance (Other) /
                      mitotic slippage (Other) / ubiquitylation (ubiquitination)
                      (Other)},
      cin          = {F045},
      ddc          = {540},
      cid          = {I:(DE-He78)F045-20160331},
      pnm          = {316 - Infektionen, Entzündung und Krebs (POF4-316)},
      pid          = {G:(DE-HGF)POF4-316},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:36395886},
      doi          = {10.1016/j.jbc.2022.102703},
      url          = {https://inrepo02.dkfz.de/record/182682},
}