
DOI . ORG {
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Title[redir]:
Phosphorylation of HDM2 by Akt | Oncogene
Description:
The HDM2 protein is a key regulator of the tumour suppressor, p53. Control of HDM2 function is critical for normal cell proliferation and stress responses, and it is becoming evident that multiple modifications of HDM2 can regulate its function within cells. In this study we show that HDM2 associated with the serine-threonine kinase, Akt, in response to growth factor stimulation of human primary cells. This association was concurrent with phosphorylation of Akt (at Ser 473), and resulted in elevated expression of HDM2 and enhanced nuclear localization. However, analysis of HDM2 proteins mutated at the consensus Akt recognition sites at serines 166 and 186 indicated that modification at these residues was not sufficient for the increased expression of the protein, which was blocked by the PI3 kinase inhibitor LY294002. Tryptic peptide and mutational analyses revealed evidence for an Akt phosphorylation site in HDM2 additional to the two consensus sites.
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nature, cell, oncogene, access, biol, article, hdm, akt, vousden, mol, content, cookies, phosphorylation, ashcroft, cancer, privacy, woods, open, levine, data, journal, march, ludwig, chem, oren, research, function, advertising, analysis, information, subscribe, copeland, weber, karen, protein, cells, expression, institution, buy, george, chen, embo, sci, usa, shifman, author, permissions, site, optional, media,
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nature portfolio permissions reprints cancer research privacy policy advertising 1992 nature 358 nature social media author information authors dual-color immunohistochemical methods author correspondence 2d phosphoamino-acid analysis personal data springerlink instant access data protection permissions privacy human primary cells issue learn serine-threonine kinase explore content subscription content cancer marta falcicchiojake akt margaret ashcroft european economic area growth factor stimulation enhanced nuclear localization institutional subscriptions read ras-camp-pka surrey sm2 5ng erg–spink1 status full-length akt accepting optional cookies normal cell proliferation cell growth laboratory journals search log article ashcroft akt phosphorylation site manage preferences https detecting erg–pten hdm2 proteins mutated content article purchase access journal publish oliver weber & karen article cite consensus sites optional cookies
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headline:Phosphorylation of HDM2 by Akt
description:The HDM2 protein is a key regulator of the tumour suppressor, p53. Control of HDM2 function is critical for normal cell proliferation and stress responses, and it is becoming evident that multiple modifications of HDM2 can regulate its function within cells. In this study we show that HDM2 associated with the serine-threonine kinase, Akt, in response to growth factor stimulation of human primary cells. This association was concurrent with phosphorylation of Akt (at Ser 473), and resulted in elevated expression of HDM2 and enhanced nuclear localization. However, analysis of HDM2 proteins mutated at the consensus Akt recognition sites at serines 166 and 186 indicated that modification at these residues was not sufficient for the increased expression of the protein, which was blocked by the PI3 kinase inhibitor LY294002. Tryptic peptide and mutational analyses revealed evidence for an Akt phosphorylation site in HDM2 additional to the two consensus sites.
datePublished:2002-03-22T00:00:00Z
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headline:Phosphorylation of HDM2 by Akt
description:The HDM2 protein is a key regulator of the tumour suppressor, p53. Control of HDM2 function is critical for normal cell proliferation and stress responses, and it is becoming evident that multiple modifications of HDM2 can regulate its function within cells. In this study we show that HDM2 associated with the serine-threonine kinase, Akt, in response to growth factor stimulation of human primary cells. This association was concurrent with phosphorylation of Akt (at Ser 473), and resulted in elevated expression of HDM2 and enhanced nuclear localization. However, analysis of HDM2 proteins mutated at the consensus Akt recognition sites at serines 166 and 186 indicated that modification at these residues was not sufficient for the increased expression of the protein, which was blocked by the PI3 kinase inhibitor LY294002. Tryptic peptide and mutational analyses revealed evidence for an Akt phosphorylation site in HDM2 additional to the two consensus sites.
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