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Description
| - Zjistili jsme že fosforylace p53 CK2 na Ser392 indukuje DNA vazebnou aktivitu p53 mnohem méně než fosforylace cdk2/cyclin A nebo PKC. Navíc jsme zjistili, že fosforylace CK2 silně inhibuje PKC indukovanou aktivaci vazby p53 na DNA, zatímco aktivace p53 cdk2/cyclin A není ovlivněna. Fosforylace CK2 zvyšuje vazbu PKC do jejího vazebného místa v p53 oligomerizační doméně, ale přitom snižuje fosforylaci p53 PKC. Tento poznatek potvrzuje, že kompetici mezi CK2 a PKC není závislá na inhibici tvorby komplexu p53-PKC. Tyto výsledky potvrzují důležitost C-koncové fosforylace při regulaci DNA vazebné aktivity proteinu p53 a současně potvrzují antagonistický vztah existující mezi rozdílnými stresovými drahami. (cs)
- We found that phosphorylation of p53 by CK2 on Ser392 induces its DNA binding aktivity of p53 to a much lower extent than phosphorylation by cdk2/cyclin A or PKC. In addition, we found that phosphorylation by CK2 strongly inhibits PKC-induced activation of p53 DNA binding, while the activation of p53 by cdk2/cyclin A is not affected by CK2. The presence of CK2-mediated phosphorylation promotes PKC binding to its docking site within the p53 oligomerization domain, but decreases phosphorylation of p53 by PKC, suggesting that competition between CK2 and PKC does not rely on the inhibition of PKC?p53 complex formation. These results indicate the crucial role of p53 C-terminal phosphorylation in the regulation of its DNA-binding activity, but also suggest that antagonistic relationships exist between different stress signalling pathways.
- We found that phosphorylation of p53 by CK2 on Ser392 induces its DNA binding aktivity of p53 to a much lower extent than phosphorylation by cdk2/cyclin A or PKC. In addition, we found that phosphorylation by CK2 strongly inhibits PKC-induced activation of p53 DNA binding, while the activation of p53 by cdk2/cyclin A is not affected by CK2. The presence of CK2-mediated phosphorylation promotes PKC binding to its docking site within the p53 oligomerization domain, but decreases phosphorylation of p53 by PKC, suggesting that competition between CK2 and PKC does not rely on the inhibition of PKC?p53 complex formation. These results indicate the crucial role of p53 C-terminal phosphorylation in the regulation of its DNA-binding activity, but also suggest that antagonistic relationships exist between different stress signalling pathways. (en)
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Title
| - Activation of DNA binding ability of latent p53 protein by protein kinase C is abolished by casein kinase II
- Aktivace DNA vazebne schopnosti latentni formy p53 protin kinasou C je inhibovana kasein kinasou II (cs)
- Activation of DNA binding ability of latent p53 protein by protein kinase C is abolished by casein kinase II (en)
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skos:prefLabel
| - Activation of DNA binding ability of latent p53 protein by protein kinase C is abolished by casein kinase II
- Aktivace DNA vazebne schopnosti latentni formy p53 protin kinasou C je inhibovana kasein kinasou II (cs)
- Activation of DNA binding ability of latent p53 protein by protein kinase C is abolished by casein kinase II (en)
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skos:notation
| - RIV/00209805:_____/04:00013927!RIV/2005/GA0/L26005/N
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http://linked.open.../vavai/riv/strany
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http://linked.open...avai/riv/aktivita
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http://linked.open...avai/riv/aktivity
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http://linked.open...iv/cisloPeriodika
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http://linked.open...vai/riv/dodaniDat
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http://linked.open...aciTvurceVysledku
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http://linked.open.../riv/druhVysledku
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http://linked.open...iv/duvernostUdaju
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http://linked.open...titaPredkladatele
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http://linked.open...dnocenehoVysledku
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http://linked.open...ai/riv/idVysledku
| - RIV/00209805:_____/04:00013927
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http://linked.open...riv/jazykVysledku
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http://linked.open.../riv/klicovaSlova
| - activation;cdk2/cyclin A;DNA binding;electrophoretic mobility shift assay (EMSA);p53;phosphorylation (en)
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http://linked.open.../riv/klicoveSlovo
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http://linked.open...odStatuVydavatele
| - GB - Spojené království Velké Británie a Severního Irska
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http://linked.open...iv/tvurceVysledku
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number of pages
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