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• W1997092292 abstract "p53 is an important regulator of cell cycle progression and apoptosis, and inactivation of p53 is associated with tumorigenesis. Although p53 exerts many of its effects through regulation of transcription, this protein is also found in association with ribosomes and several mRNAs have been identified that are translationally controlled in a p53-dependent manner. We have utilized murine erythroleukemic cells that express a temperature-sensitive p53 protein to determine whether p53 also functions at the level of translation. The data presented here demonstrate that p53 causes a rapid decrease in translation initiation. Analysis of several potential mechanisms for regulating protein synthesis shows that p53 has selective effects on the phosphorylation of the eIF4E-binding protein, 4E-BP1, and the activity of the p70 ribosomal protein S6 kinase. These data provide evidence that modulation of translational activity constitutes a further mechanism by which the growth inhibitory effects of p53 may be mediated." @default.
• W1997092292 created "2016-06-24" @default.
• W1997092292 creator A5005620487 @default.
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• W1997092292 creator A5029919366 @default.
• W1997092292 creator A5078698929 @default.
• W1997092292 creator A5087414735 @default.
• W1997092292 date "2002-08-02" @default.
• W1997092292 modified "2023-10-11" @default.
• W1997092292 title "p53 activation results in rapid dephosphorylation of the eIF4E-binding protein 4E-BP1, inhibition of ribosomal protein S6 kinase and inhibition of translation initiation" @default.
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• W1997092292 doi "https://doi.org/10.1038/sj.onc.1205662" @default.
• W1997092292 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/12149653" @default.
• W1997092292 hasPublicationYear "2002" @default.
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