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Verfasst von:Di Ventura, Barbara [VerfasserIn]   i
 Knop, Michael [VerfasserIn]   i
Titel:Reconstitution of Mdm2-dependent post-translational modifications of p53 in yeast
Verf.angabe:Barbara Di Ventura, Charlotta Funaya, Claude Antony, Michael Knop, Luis Serrano
Fussnoten:Gesehen am 15.08.2017
Titel Quelle:Enthalten in: Public Library of Science: PLoS one
Jahr Quelle:2008
Band/Heft Quelle:3(2008,1) Artikel-Nummer e1507, 9 Seiten
ISSN Quelle:1932-6203
Abstract:p53 mediates cell cycle arrest or apoptosis in response to DNA damage. Its activity is subject to a tight regulation involving a multitude of post-translational modifications. The plethora of functional protein interactions of p53 at present precludes a clear understanding of regulatory principles in the p53 signaling network. To circumvent this complexity, we studied here the minimal requirements for functionally relevant p53 post-translational modifications by expressing human p53 together with its best characterized modifier Mdm2 in budding yeast. We find that expression of the human p53-Mdm2 module in yeast is sufficient to faithfully recapitulate key aspects of p53 regulation in higher eukaryotes, such as Mdm2-dependent targeting of p53 for degradation, sumoylation at lysine 386 and further regulation of this process by p14ARF. Interestingly, sumoylation is necessary for the recruitment of p53-Mdm2 complexes to yeast nuclear bodies morphologically akin to human PML bodies. These results suggest a novel role for Mdm2 as well as for p53 sumoylation in the recruitment of p53 to nuclear bodies. The reductionist yeast model that was established and validated in this study will now allow to incrementally study simplified parts of the intricate p53 network, thus helping elucidate the core mechanisms of p53 regulation as well as test novel strategies to counteract p53 malfunctions.
DOI:doi:10.1371/journal.pone.0001507
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Kostenfrei: Verlag: http://dx.doi.org/10.1371/journal.pone.0001507
 Kostenfrei: Verlag: http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0001507
 DOI: https://doi.org/10.1371/journal.pone.0001507
Datenträger:Online-Ressource
Sprache:eng
K10plus-PPN:1562427628
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