title: Stabilization of alanine substituted p53 protein at Ser15, Thr18, and Ser20 in response to ionizing radiation.
abstract: Phosphorylation of p53 at Ser15, Thr18, and Ser20 has been thought to be important for p53 stabilization in response to ionizing radiation. In the present study, we examined the X-ray-induced stabilization of Ala-substituted p53 protein at Ser15, Thr18, and Ser20, whose gene expression was controlled under an ecdyson-inducible promoter. We found that all single-, double-, or triple-Ala-substituted p53 at Ser15, Yhr18, and Ser20 were accumulated in the nucleus similarly to wild-type p53 after X-irradiation. These results indicate that the phosphorylation of p53 at Ser15, Thr18, and Ser20 is not necessarily needed for p53 stabilization in response to ionizing radiation.
authors.affiliation: Division of Radiation Biology, Department of Radiology and Radiation Biology, Graduate School of Biomedical Sciences, Nagasaki University, 1-14 Bunkyo-machi, Nagasaki 852-8521, Japan.
authors.forename: Motohiro
authors.initials: M
authors.lastname: Yamauchi
authors.forename: Keiji
authors.initials: K
authors.lastname: Suzuki
authors.forename: Seiji
authors.initials: S
authors.lastname: Kodama
authors.forename: Masami
authors.initials: M
authors.lastname: Watanabe
mesh_terms: D000409:Alanine / Q000378:metabolism* / Q000528:radiation effects*; D019943:Amino Acid Substitution; D002289:Carcinoma, Non-Small-Cell Lung / Q000378:metabolism*; D045744:Cell Line, Tumor; D005354:Fibrosarcoma / Q000378:metabolism*; D015972:Gene Expression Regulation, Neoplastic / Q000528:radiation effects*; D006801:Humans; D016297:Mutagenesis, Site-Directed; D011829:Radiation Dosage; D011839:Radiation, Ionizing; D011994:Recombinant Proteins / Q000378:metabolism; D013329:Structure-Activity Relationship; D016159:Tumor Suppressor Protein p53 / Q000378:metabolism* / Q000528:radiation effects*
chemical_list: D011994:Recombinant Proteins; D016159:Tumor Suppressor Protein p53; D000409:Alanine