Meek D W
Biomedical Research Centre, Ninewells Hospital and Medical School, Dundee, UK.
Semin Cancer Biol. 1994 Jun;5(3):203-10.
The p53 tumor suppressor protein is extensively post-translationally modified, mostly by phosphorylation. The phosphorylation sites are clustered into two distinct domains within the p53 polypeptide and the protein kinases and phosphatases which modify many of these sites have been identified. In addition, signaling pathways which modulate the phosphorylation state of p53, leading perhaps to changes in its activity, are being actively investigated. Similarly, the transforming proteins of DNA tumor viruses modulate p53 phosphorylation and may therefore be useful tools for probing these regulatory mechanisms. Given the very potent effects of p53 on cell growth and the extent of phosphorylation of this protein, p53 may well be controlled tightly and coordinately by more than one signaling mechanism.
p53肿瘤抑制蛋白在翻译后会发生广泛修饰，主要是磷酸化修饰。磷酸化位点集中在p53多肽的两个不同结构域内，并且已经鉴定出修饰其中许多位点的蛋白激酶和磷酸酶。此外，正在积极研究调节p53磷酸化状态从而可能导致其活性变化的信号通路。同样，DNA肿瘤病毒的转化蛋白可调节p53磷酸化，因此可能是探究这些调控机制的有用工具。鉴于p53对细胞生长具有非常强大的作用以及该蛋白的磷酸化程度，p53很可能受到不止一种信号机制的严格且协同的调控。
