Aurora-A phosphorylates hnRNPK and disrupts its interaction with p53

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• 作者：Kai-Wei Hsueh^a ; Shu-Ling Fu^b ; Chi-Ying F. Huang^c ; Chao-Hsiung Lin^a ; ^{chlin2@ym.edu.tw}
• 关键词：Aurora-A ; hnRNPK ; p53 Interaction
• 刊名：FEBS Letters
• 出版年：2011
• 出版时间：2 September, 2011
• 年：2011
• 卷：585
• 期：17
• 页码：2671-2675
• 全文大小：1K

文摘

Amplification of Aurora-A, encoding a cell cycle-regulating kinase, has been reported in human cancers. Although Aurora-A is known to directly phosphorylate and down-regulate p53, the detailed mechanism remains unclear. Here we show that Aurora-A phosphorylates hnRNPK, a transcriptional coactivator of p53, on serine 379. This phosphorylation does not affect the post-transcriptional activity or cellular localization of hnRNPK, but disrupts its interaction with p53. Inverse correlation between Aurora-A activity and hnRNPK-p53 interaction was further demonstrated in DNA-damaged cells. Our results provide an alternative mechanism, whereby via phosphorylating hnRNPK Aurora-A participates in regulating p53 activity during DNA damage.

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