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Statements

Subject Item
n2:RIV%2F00209805%3A_____%2F04%3A00013927%21RIV%2F2005%2FGA0%2FL26005%2FN
rdf:type
n15:Vysledek skos:Concept
dcterms:description
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. 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.
dcterms:title
Activation of DNA binding ability of latent p53 protein by protein kinase C is abolished by casein kinase II 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
skos:prefLabel
Activation of DNA binding ability of latent p53 protein by protein kinase C is abolished by casein kinase II 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
skos:notation
RIV/00209805:_____/04:00013927!RIV/2005/GA0/L26005/N
n6:strany
939; 947
n6:aktivita
n14:P
n6:aktivity
P(GA301/02/0831)
n6:cisloPeriodika
pt. 3
n6:dodaniDat
n7:2005
n6:domaciTvurceVysledku
n9:9637419
n6:druhVysledku
n17:J
n6:duvernostUdaju
n11:S
n6:entitaPredkladatele
n13:predkladatel
n6:idSjednocenehoVysledku
553448
n6:idVysledku
RIV/00209805:_____/04:00013927
n6:jazykVysledku
n16:eng
n6:klicovaSlova
activation;cdk2/cyclin A;DNA binding;electrophoretic mobility shift assay (EMSA);p53;phosphorylation
n6:klicoveSlovo
n8:DNA%20binding n8:electrophoretic%20mobility%20shift%20assay%20%28EMSA%29 n8:cdk2%2Fcyclin%20A n8:activation n8:phosphorylation n8:p53
n6:kodStatuVydavatele
GB - Spojené království Velké Británie a Severního Irska
n6:kontrolniKodProRIV
[F9F4EDC19AAF]
n6:nazevZdroje
The Biochemical journal
n6:obor
n12:FD
n6:pocetDomacichTvurcuVysledku
2
n6:pocetTvurcuVysledku
8
n6:projekt
n10:GA301%2F02%2F0831
n6:rokUplatneniVysledku
n7:2004
n6:svazekPeriodika
378
n6:tvurceVysledku
Vojtěšek, Bořivoj
s:issn
0264-6021
s:numberOfPages
9