S100A6 与 p300 的 TAZ2 结构域竞争结合 p53，并减弱 p53 的乙酰化。
S100A6 competes with the TAZ2 domain of p300 for binding to p53 and attenuates p53 acetylation.
机构信息
Nencki Institute of Experimental Biology, 3 Pasteur Street, 02-093 Warsaw, Poland.
出版信息
J Mol Biol. 2013 Sep 23;425(18):3488-94. doi: 10.1016/j.jmb.2013.06.007. Epub 2013 Jun 22.
S100A6 is a calcium binding protein that, like some other members of the S100 protein family, is able to bind p53. This interaction may be physiologically relevant considering the numerous connotations of S100 proteins and of S100A6, in particular, with cancer and metastasis. In this work, we show that the interaction with S100A6 is limited to unmodified or phosphorylated p53 and is inhibited by p53 acetylation. Using in vitro acetylation assay, we show that the presence of S100A6 attenuates p53 acetylation by p300. Furthermore, using ELISA, we show that S100A6 and the TAZ2 domain of p300 bind p53 with similar affinities and that S100A6 effectively competes with TAZ2 for binding to p53. Our results add another element to the complicated scheme of p53 activation.
S100A6 是一种钙结合蛋白，与 S100 蛋白家族的其他一些成员一样，能够与 p53 结合。考虑到 S100 蛋白和 S100A6 的众多含义，特别是与癌症和转移的关系，这种相互作用可能具有生理相关性。在这项工作中，我们表明与 S100A6 的相互作用仅限于未修饰或磷酸化的 p53，并且受到 p53 乙酰化的抑制。使用体外乙酰化测定法，我们表明 S100A6 存在会减弱 p300 对 p53 的乙酰化作用。此外，使用 ELISA，我们表明 S100A6 和 p300 的 TAZ2 结构域与 p53 具有相似的亲和力，并且 S100A6 可以有效地与 TAZ2 竞争与 p53 的结合。我们的结果为 p53 激活的复杂方案增加了另一个要素。
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