Stabilization of alanine substituted p53 protein at Ser15, Thr18, and Ser20 in response to ionizing radiation.
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.
Yamauchi
Motohiro
M
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.
Suzuki
Keiji
K
Kodama
Seiji
S
Watanabe
Masami
M
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*
D011994:Recombinant Proteins; D016159:Tumor Suppressor Protein p53; D000409:Alanine