Aktivace DNA vazebne schopnosti latentni formy p53 protin kinasou C je inhibovana kasein kinasou II

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00209805%3A_____%2F04%3A00013927" target="_blank" >RIV/00209805:_____/04:00013927 - isvavai.cz</a>

Výsledek na webu

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DOI - Digital Object Identifier

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Jazyk výsledku

angličtina

Název v původním jazyce

Activation of DNA binding ability of latent p53 protein by protein kinase C is abolished by casein kinase II

Popis výsledku v původním jazyce

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 activationof 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 byPKC, 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.

Název v anglickém jazyce

Activation of DNA binding ability of latent p53 protein by protein kinase C is abolished by casein kinase II

Popis výsledku anglicky

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 activationof 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 byPKC, 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.

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

FD - Onkologie a hematologie

OECD FORD obor

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Projekt

<a href="/cs/project/GA301%2F02%2F0831" target="_blank" >GA301/02/0831: Interakce proteinu p53 a jeho homologů a DNA a jejich úloha v maligní transformaci</a><br>

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2004

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

The Biochemical journal

ISSN

0264-6021

e-ISSN

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Svazek periodika

378

Číslo periodika v rámci svazku

pt. 3

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

9

Strana od-do

939-947

Kód UT WoS článku

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EID výsledku v databázi Scopus

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