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000127374 0247_ $$2doi$$a10.1074/jbc.M114.628982
000127374 0247_ $$2pmid$$apmid:25944899
000127374 0247_ $$2pmc$$apmc:PMC4505402
000127374 0247_ $$2ISSN$$a0021-9258
000127374 0247_ $$2ISSN$$a1083-351X
000127374 037__ $$aDKFZ-2017-03399
000127374 041__ $$aeng
000127374 082__ $$a570
000127374 1001_ $$aReuven, Nina$$b0
000127374 245__ $$aThe Tyrosine Kinase c-Abl Promotes Homeodomain-interacting Protein Kinase 2 (HIPK2) Accumulation and Activation in Response to DNA Damage.
000127374 260__ $$aBethesda, Md.$$bSoc.$$c2015
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000127374 520__ $$aThe 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.
000127374 536__ $$0G:(DE-HGF)POF3-311$$a311 - Signalling pathways, cell and tumor biology (POF3-311)$$cPOF3-311$$fPOF III$$x0
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000127374 650_7 $$2NLM Chemicals$$aCarrier Proteins
000127374 650_7 $$2NLM Chemicals$$aTumor Suppressor Protein p53
000127374 650_7 $$0EC 2.7.1.-$$2NLM Chemicals$$aHIPK2 protein, human
000127374 650_7 $$0EC 2.7.10.2$$2NLM Chemicals$$aProto-Oncogene Proteins c-abl
000127374 650_7 $$0EC 2.7.11.1$$2NLM Chemicals$$aProtein-Serine-Threonine Kinases
000127374 7001_ $$aAdler, Julia$$b1
000127374 7001_ $$aPorat, Ziv$$b2
000127374 7001_ $$0P:(DE-HGF)0$$aPolonio-Vallon, Tilman$$b3
000127374 7001_ $$0P:(DE-He78)99ae95278bd95e30462a4fb2d12026c6$$aHofmann, Thomas$$b4$$udkfz
000127374 7001_ $$aShaul, Yosef$$b5
000127374 773__ $$0PERI:(DE-600)1474604-9$$a10.1074/jbc.M114.628982$$gVol. 290, no. 27, p. 16478 - 16488$$n27$$p16478 - 16488$$tThe journal of biological chemistry$$v290$$x1083-351X$$y2015
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000127374 9141_ $$y2015
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