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H. Feng, X.–Q. Huang, Y. Liu, J.–P. Liu, S.–J. Liu, C. Luo, Y. Liu, D.W. Li; Dephosphorylation of the Tumor Suppressor, p53, at the N–terminal Serine/Threonine Sites Modulates Its Transactivity and Apoptotic Ability . Invest. Ophthalmol. Vis. Sci. 2004;45(13):402.
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© ARVO (1962-2015); The Authors (2016-present)
Purpose: Our previous studies have demonstrated that protein phosphatase–1 (PP–1) is important in promoting survival of lens epithelial cells. Recent studies have revealed that PP–1 may exert its antiapoptotic function through dephosphorylation of p53. In the present study, we have compared the function of wild type and mutated p53 in mediating transactivation and apoptosis in lens and non–lens cells. Methods: PCR–linked in vitro mutagenesis was used to generate the following mutations: S15A and S20A. The function of these mutants in regulating apoptosis and also expression of the downstream apoptosis–related genes were compared with wild type p53 in human lens epithelial cells with p53 knocked out and p53 –/– tumor cell line, DU145. Results: Mutation of the phosphorylation sites at Ser–15 and Ser–20 modulates both the transactivity and apoptotic ability of p53. Conclusions: Dephosphorylation of p53 plays an role in its function mediating apoptosis. Supported by the Hormel Foundation, University of Minnesota Graduate School and Lotus Scholar Professorship funds from Hunan Normal University. None.
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