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@ARTICLE{Oh:130276,
      author       = {S. Oh and R. A. Flynn and S. N. Floor and J. Purzner and L.
                      Martin and B. T. Do and S. Schubert and D. Vaka and S.
                      Morrissy and Y. Li and M. Kool$^*$ and V. Hovestadt$^*$ and
                      D. Jones$^*$ and P. A. Northcott$^*$ and T. Risch and H.-J.
                      Warnatz and M.-L. Yaspo and C. M. Adams and R. D. Leib and
                      M. Breese and M. A. Marra and D. Malkin and P. Lichter$^*$
                      and J. A. Doudna and S. Pfister$^*$ and M. D. Taylor and H.
                      Y. Chang and Y.-J. Cho},
      title        = {{M}edulloblastoma-associated {DDX}3 variant selectively
                      alters the translational response to stress.},
      journal      = {OncoTarget},
      volume       = {7},
      number       = {19},
      issn         = {1949-2553},
      address      = {[S.l.]},
      publisher    = {Impact Journals LLC},
      reportid     = {DKFZ-2017-05355},
      pages        = {28169 - 28182},
      year         = {2016},
      abstract     = {DDX3X encodes a DEAD-box family RNA helicase (DDX3)
                      commonly mutated in medulloblastoma, a highly aggressive
                      cerebellar tumor affecting both children and adults. Despite
                      being implicated in several facets of RNA metabolism, the
                      nature and scope of DDX3s interactions with RNA remain
                      unclear. Here, we show DDX3 collaborates extensively with
                      the translation initiation machinery through direct binding
                      to 5UTRs of nearly all coding RNAs, specific sites on the
                      18S rRNA, and multiple components of the translation
                      initiation complex. Impairment of translation initiation is
                      also evident in primary medulloblastomas harboring mutations
                      in DDX3X, further highlighting DDX3s role in this process.
                      Arsenite-induced stress shifts DDX3 binding from the 5UTR
                      into the coding region of mRNAs concomitant with a general
                      reduction of translation, and both the shift of DDX3 on mRNA
                      and decreased translation are blunted by expression of a
                      catalytically-impaired, medulloblastoma-associated DDX3R534H
                      variant. Furthermore, despite the global repression of
                      translation induced by arsenite, translation is preserved on
                      select genes involved in chromatin organization in
                      DDX3R534H-expressing cells. Thus, DDX3 interacts extensively
                      with RNA and ribosomal machinery to help remodel the
                      translation landscape in response to stress, while
                      cancer-related DDX3 variants adapt this response to
                      selectively preserve translation.},
      cin          = {B062 / B060},
      ddc          = {610},
      cid          = {I:(DE-He78)B062-20160331 / I:(DE-He78)B060-20160331},
      pnm          = {312 - Functional and structural genomics (POF3-312)},
      pid          = {G:(DE-HGF)POF3-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:27058758},
      pmc          = {pmc:PMC5053718},
      doi          = {10.18632/oncotarget.8612},
      url          = {https://inrepo02.dkfz.de/record/130276},
}