About: Activation of DNA binding ability of latent p53 protein by protein kinase C is abolished by casein kinase II     Goto   Sponge   NotDistinct   Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

AttributesValues
rdf:type
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)
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)
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)
skos:notation
  • RIV/00209805:_____/04:00013927!RIV/2005/GA0/L26005/N
http://linked.open.../vavai/riv/strany
  • 939; 947
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(GA301/02/0831)
http://linked.open...iv/cisloPeriodika
  • pt. 3
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 553448
http://linked.open...ai/riv/idVysledku
  • RIV/00209805:_____/04:00013927
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • activation;cdk2/cyclin A;DNA binding;electrophoretic mobility shift assay (EMSA);p53;phosphorylation (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • GB - Spojené království Velké Británie a Severního Irska
http://linked.open...ontrolniKodProRIV
  • [F9F4EDC19AAF]
http://linked.open...i/riv/nazevZdroje
  • The Biochemical journal
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 378
http://linked.open...iv/tvurceVysledku
  • Vojtěšek, Bořivoj
issn
  • 0264-6021
number of pages
Faceted Search & Find service v1.16.118 as of Jun 21 2024


Alternative Linked Data Documents: ODE     Content Formats:   [cxml] [csv]     RDF   [text] [turtle] [ld+json] [rdf+json] [rdf+xml]     ODATA   [atom+xml] [odata+json]     Microdata   [microdata+json] [html]    About   
This material is Open Knowledge   W3C Semantic Web Technology [RDF Data] Valid XHTML + RDFa
OpenLink Virtuoso version 07.20.3240 as of Jun 21 2024, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (126 GB total memory, 47 GB memory in use)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software