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- W2355672715 abstract "Objective To explore the role of p53 acetylation at Lys370 in mediating p53 transactivation and its proapoptotic effect under UVB exposure.Methods Wild type(wt) and p53-/-murine embryonic fibroblasts(MEFs) were exposed to UVB.Luciferase assay was used to detect the transactivation of p53.The accumulation and acetylation of p53 at Lys370 in the UVB response were tested by Western-blot assay.p53-/-MEFs were transfected with the plasmids containing wild-type p53(wt p53) or p53 with a Lys370Arg mutation(K370R) generated by mutagenic PCR and exposed to UVB,then the transactivation of p53 was detected by the luciferase assay,and the apoptosis of transfected cells was determined by a flow cytometric assay.Results Both dose-and time-dependent experiments indicated a significant increase of p53 transactivity under UVB exposure,along with the strong induction of p53 acetylation at Lys370 under the same conditions.Abrogation of p53 acetylation at Lys370 by mutagenesis did not affect p53 protein stability but remarkably decreased UVB-induced transactivation of p53 and the apoptotic response.Conclusion p53 Acetylation at Lys370 plays an important role in the transactivation of p53 and the induced apoptotic response under UVB exposure." @default.
- W2355672715 created "2016-06-24" @default.
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- W2355672715 date "2011-01-01" @default.
- W2355672715 modified "2023-09-26" @default.
- W2355672715 title "Acetylation at K370 is critical for mediating p53 transactivation and apoptotic response under UVB exposure" @default.
- W2355672715 hasPublicationYear "2011" @default.
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