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    FEBS Lett. 2011 Sep 2;585(17):2671-5. Epub 2011 Aug 3.

    Aurora-A phosphorylates hnRNPK and disrupts its interaction with p53.

    Hsueh KW, Fu SL, Huang CY, Lin CH.

    Source

    Department of Life Sciences and Institute of Genome Sciences, National Yang-Ming University, Taipei, Taiwan.

    Abstract

    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.

    Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.

    PMID:
    21821029
    [PubMed - indexed for MEDLINE]

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