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A p53 amino-terminal nuclear export signal inhibited by DNA damage-induced phosphorylation

Zhang, Y ; Xiong, Y

Science (New York, N.Y.), 08 June 2001, Vol.292(5523), pp.1910-5 [Tạp chí có phản biện]

ISSN: 0036-8075 ; PMID: 11397945 Version:1

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  • Nhan đề:
    A p53 amino-terminal nuclear export signal inhibited by DNA damage-induced phosphorylation
  • Tác giả: Zhang, Y ; Xiong, Y
  • Chủ đề: DNA Damage ; Nuclear Proteins ; Protein Sorting Signals ; Cell Nucleus -- Metabolism ; Tumor Suppressor Protein P53 -- Chemistry
  • Là 1 phần của: Science (New York, N.Y.), 08 June 2001, Vol.292(5523), pp.1910-5
  • Mô tả: The p53 protein is present in low amounts in normally growing cells and is activated in response to physiological insults. MDM2 regulates p53 either through inhibiting p53's transactivating function in the nucleus or by targeting p53 degradation in the cytoplasm. We identified a previously unknown nuclear export signal (NES) in the amino terminus of p53, spanning residues 11 to 27 and containing two serine residues phosphorylated after DNA damage, which was required for p53 nuclear export in colloboration with the carboxyl-terminal NES. Serine-15-phosphorylated p53 induced by ultraviolet irradiation was not exported. Thus, DNA damage-induced phosphorylation may achieve optimal p53 activation by inhibiting both MDM2 binding to, and the nuclear export of, p53.
  • Ngôn ngữ: English
  • Số nhận dạng: ISSN: 0036-8075 ; PMID: 11397945 Version:1

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