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@ARTICLE{Reuven:127374,
      author       = {N. Reuven and J. Adler and Z. Porat and T.
                      Polonio-Vallon$^*$ and T. Hofmann$^*$ and Y. Shaul},
      title        = {{T}he {T}yrosine {K}inase c-{A}bl {P}romotes
                      {H}omeodomain-interacting {P}rotein {K}inase 2 ({HIPK}2)
                      {A}ccumulation and {A}ctivation in {R}esponse to {DNA}
                      {D}amage.},
      journal      = {The journal of biological chemistry},
      volume       = {290},
      number       = {27},
      issn         = {1083-351X},
      address      = {Bethesda, Md.},
      publisher    = {Soc.},
      reportid     = {DKFZ-2017-03399},
      pages        = {16478 - 16488},
      year         = {2015},
      abstract     = {The non-receptor tyrosine kinase c-Abl is activated in
                      response to DNA damage and induces p73-dependent apoptosis.
                      Here, we investigated c-Abl regulation of the
                      homeodomain-interacting protein kinase 2 (HIPK2), an
                      important regulator of p53-dependent apoptosis. c-Abl
                      phosphorylated HIPK2 at several sites, and phosphorylation
                      by c-Abl protected HIPK2 from degradation mediated by the
                      ubiquitin E3 ligase Siah-1. c-Abl and HIPK2 synergized in
                      activating p53 on apoptotic promoters in a reporter assay,
                      and c-Abl was required for endogenous HIPK2 accumulation and
                      phosphorylation of p53 at Ser(46) in response to DNA damage
                      by γ- and UV radiation. Accumulation of HIPK2 in nuclear
                      speckles and association with promyelocytic leukemia protein
                      (PML) in response to DNA damage were also dependent on c-Abl
                      activity. At high cell density, the Hippo pathway inhibits
                      DNA damage-induced c-Abl activation. Under this condition,
                      DNA damage-induced HIPK2 accumulation, phosphorylation of
                      p53 at Ser(46), and apoptosis were attenuated. These data
                      demonstrate a new mechanism for the induction of DNA
                      damage-induced apoptosis by c-Abl and illustrate network
                      interactions between serine/threonine and tyrosine kinases
                      that dictate cell fate.},
      keywords     = {Carrier Proteins (NLM Chemicals) / Tumor Suppressor Protein
                      p53 (NLM Chemicals) / HIPK2 protein, human (NLM Chemicals) /
                      Proto-Oncogene Proteins c-abl (NLM Chemicals) /
                      Protein-Serine-Threonine Kinases (NLM Chemicals)},
      cin          = {A210},
      ddc          = {570},
      cid          = {I:(DE-He78)A210-20160331},
      pnm          = {311 - Signalling pathways, cell and tumor biology
                      (POF3-311)},
      pid          = {G:(DE-HGF)POF3-311},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {pmid:25944899},
      pmc          = {pmc:PMC4505402},
      doi          = {10.1074/jbc.M114.628982},
      url          = {https://inrepo02.dkfz.de/record/127374},
}