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@ARTICLE{Rajagopal:299577,
      author       = {V. Rajagopal$^*$ and J. S. Seiler$^*$ and I. Nasa and S.
                      Cantarella$^*$ and J. Theiss$^*$ and F. Herget$^*$ and B.
                      Kaifer$^*$ and M. Klostermann and R. Will$^*$ and M.
                      Schneider$^*$ and D. Helm$^*$ and J. König and K. Zarnack
                      and S. Diederichs$^*$ and A. N. Kettenbach and M.
                      Caudron-Herger$^*$},
      title        = {{A}n atlas of {RNA}-dependent proteins in cell division
                      reveals the riboregulation of mitotic protein-protein
                      interactions.},
      journal      = {Nature Communications},
      volume       = {16},
      number       = {1},
      issn         = {2041-1723},
      address      = {[London]},
      publisher    = {Springer Nature},
      reportid     = {DKFZ-2025-00518},
      pages        = {2325},
      year         = {2025},
      note         = {#EA:B150#LA:B150#},
      abstract     = {Ribonucleoprotein complexes are dynamic assemblies of RNA
                      with RNA-binding proteins, which modulate the fate of RNA.
                      Inversely, RNA riboregulates the interactions and functions
                      of the associated proteins. Dysregulation of
                      ribonucleoprotein functions is linked to diseases such as
                      cancer and neurological disorders. In dividing cells, RNA
                      and RNA-binding proteins are present in mitotic structures,
                      but their impact on cell division remains unclear. By
                      applying the proteome-wide R-DeeP strategy to cells
                      synchronized in mitosis versus interphase integrated with
                      the RBP2GO knowledge, we provided an atlas of RNA-dependent
                      proteins in cell division, accessible at R-DeeP3.dkfz.de. We
                      uncovered AURKA, KIFC1 and TPX2 as unconventional
                      RNA-binding proteins. KIFC1 was identified as a new
                      substrate of AURKA, and new TPX2-interacting protein. Their
                      pair-wise interactions were RNA dependent. In addition, RNA
                      stimulated AURKA kinase activity and stabilized its
                      conformation. In this work, we highlighted riboregulation of
                      major mitotic factors as an additional complexity level of
                      cell division.},
      keywords     = {Humans / Aurora Kinase A: metabolism / Aurora Kinase A:
                      genetics / Mitosis / Cell Cycle Proteins: metabolism / Cell
                      Cycle Proteins: genetics / Microtubule-Associated Proteins:
                      metabolism / Microtubule-Associated Proteins: genetics /
                      RNA-Binding Proteins: metabolism / RNA-Binding Proteins:
                      genetics / HeLa Cells / RNA: metabolism / RNA: genetics /
                      Protein Binding / Cell Division / Nuclear Proteins:
                      metabolism / Nuclear Proteins: genetics / Proteome:
                      metabolism / Aurora Kinase A (NLM Chemicals) / Cell Cycle
                      Proteins (NLM Chemicals) / Microtubule-Associated Proteins
                      (NLM Chemicals) / TPX2 protein, human (NLM Chemicals) /
                      RNA-Binding Proteins (NLM Chemicals) / RNA (NLM Chemicals) /
                      AURKA protein, human (NLM Chemicals) / Nuclear Proteins (NLM
                      Chemicals) / Proteome (NLM Chemicals)},
      cin          = {B150 / W111 / W120 / FR01},
      ddc          = {500},
      cid          = {I:(DE-He78)B150-20160331 / I:(DE-He78)W111-20160331 /
                      I:(DE-He78)W120-20160331 / I:(DE-He78)FR01-20160331},
      pnm          = {312 - Funktionelle und strukturelle Genomforschung
                      (POF4-312)},
      pid          = {G:(DE-HGF)POF4-312},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:40057470},
      pmc          = {pmc:PMC11890761},
      doi          = {10.1038/s41467-025-57671-3},
      url          = {https://inrepo02.dkfz.de/record/299577},
}