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@ARTICLE{Hirth:291567,
      author       = {A. Hirth$^*$ and E. Fatti$^*$ and E. Netz and S. P.
                      Acebron$^*$ and D. Papageorgiou$^*$ and A. Svorinic$^*$ and
                      C.-M. Cruciat$^*$ and E. Karaulanov and A. Gopanenko and T.
                      Zhu$^*$ and I. Sinning and J. Krijgsveld$^*$ and O.
                      Kohlbacher and C. Niehrs$^*$},
      title        = {{DEAD} box {RNA} helicases are pervasive protein kinase
                      interactors and activators.},
      journal      = {Genome research},
      volume       = {34},
      number       = {6},
      issn         = {1054-9803},
      address      = {Cold Spring Harbor, NY},
      publisher    = {Laboratory Press},
      reportid     = {DKFZ-2024-01452},
      pages        = {952-966},
      year         = {2024},
      note         = {DKFZ-ZMBH Alliance / #EA:A050#LA:A050# / 2024 Jul
                      23;34(6):952-966},
      abstract     = {DEAD box (DDX) RNA helicases are a large family of ATPases,
                      many of which have unknown functions. There is emerging
                      evidence that besides their role in RNA biology, DDX
                      proteins may stimulate protein kinases. To investigate if
                      protein kinase-DDX interaction is a more widespread
                      phenomenon, we conducted three orthogonal large-scale
                      screens, including proteomics analysis with 32 RNA
                      helicases, protein array profiling, and kinome-wide in vitro
                      kinase assays. We retrieved Ser/Thr protein kinases as
                      prominent interactors of RNA helicases and report hundreds
                      of binary interactions. We identified members of ten protein
                      kinase families, which bind to, and are stimulated by, DDX
                      proteins, including CDK, CK1, CK2, DYRK, MARK, NEK, PRKC,
                      SRPK, STE7/MAP2K, and STE20/PAK family members. We
                      identified MARK1 in all screens and validated that DDX
                      proteins accelerate the MARK1 catalytic rate. These findings
                      indicate pervasive interactions between protein kinases and
                      DEAD box RNA helicases, and provide a rich resource to
                      explore their regulatory relationships.},
      cin          = {B230 / A050},
      ddc          = {540},
      cid          = {I:(DE-He78)B230-20160331 / I:(DE-He78)A050-20160331},
      pnm          = {311 - Zellbiologie und Tumorbiologie (POF4-311)},
      pid          = {G:(DE-HGF)POF4-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:38986579},
      doi          = {10.1101/gr.278264.123},
      url          = {https://inrepo02.dkfz.de/record/291567},
}