hnRNP-U is a specific DNA-dependent protein kinase substrate phosphorylated in response to DNA double-strand breaks

Fredrik M. Berglund, Paul R. Clarke

    Research output: Contribution to journalArticle

    23 Citations (Scopus)

    Abstract

    Cellular responses to DNA damage are orchestrated by the large phosphoinositol-3-kinase related kinases ATM, ATR and DNA-PK. We have developed a cell-free system to dissect the biochemical mechanisms of these kinases. Using this system, we identify heterogeneous nuclear ribonucleoprotein U (hnRNP-U), also termed scaffold attachment factor A (SAF-A), as a specific substrate for DNA-PK. We show that hnRNP-U is phosphorylated at Ser59 by DNA-PK in vitro and in cells in response to DNA double-strand breaks. Phosphorylation of hnRNP-U suggests novel functions for DNA-PK in the response to DNA damage. (C) 2009 Elsevier Inc. All rights reserved.

    Original languageEnglish
    Pages (from-to)59-64
    Number of pages6
    JournalBiochemical and Biophysical Research Communications
    Volume381
    Issue number1
    DOIs
    Publication statusPublished - 27 Mar 2009

    Keywords

    • DNA-PK
    • hnRNP-U
    • SAF-A
    • DNA damage
    • Etoposide
    • MESSENGER-RNA
    • ATM
    • PK
    • CHK1
    • IDENTIFICATION
    • CHECKPOINT
    • ACTIVATION
    • INHIBITOR
    • RADIATION
    • MUTATION

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