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首页> 外文期刊>Journal of Molecular Biology >S100A6 competes with the TAZ2 domain of p300 for binding to p53 and attenuates p53 acetylation
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S100A6 competes with the TAZ2 domain of p300 for binding to p53 and attenuates p53 acetylation

机译:S100A6与p300的TAZ2结构域竞争结合p53并减弱p53乙酰化

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摘要

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.
机译:S100A6是一种钙结合蛋白,与S100蛋白家族的其他成员一样,能够结合p53。考虑到S100蛋白和S100A6的许多含义,特别是与癌症和转移有关,这种相互作用在生理上可能是相关的。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,并被p53乙酰化所抑制。使用体外乙酰化测定,我们显示S100A6的存在通过p300减弱了p53乙酰化。此外,使用ELISA,我们显示S100A6和p300的TAZ2结构域以相似的亲和力结合p53,并且S100A6与TAZ2有效竞争与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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