DAZAP1 interacts via its RNA-recognition motifs with the C-termini of other RNA-binding proteins

Huei-Ting Yang, Mark Peggie, Philip Cohen, Simon Rousseau

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    16 Citations (Scopus)

    Abstract

    The turnover and translation of many human mRNAs is regulated by AU-rich elements present in their 3'-untranslated region, which bind various trans acting factors. We previously identified a trans acting factor that interacts with these cis elements as DAZAP1 (deleted in Azoospermia (DAZ)-Associated Protein 1), whose interaction with the germ cell-specific protein DAZ was disrupted by the phosphorylation of DAZAP1. Here we have identified several other RNA-binding proteins as binding partners for DAZAP1 in non-germinal cells. Unlike DAZ, these interactions Occur between the RNA recognition motifs of DAZAP1 and the C-termini of the binding partners and in a phosphorylation-independent manner. The results suggest that DAZAP1 is a component of complexes that are crucial for the degradation and silencing of mRNA. (C) 2009 Elsevier Inc. All rights reserved.

    Original languageEnglish
    Pages (from-to)705-709
    Number of pages5
    JournalBiochemical and Biophysical Research Communications
    Volume380
    Issue number3
    DOIs
    Publication statusPublished - 13 Mar 2009

    Keywords

    • mRNA
    • AU-rich element
    • hnRNP
    • Translation
    • Protein-protein interaction
    • ALPHA MESSENGER-RNA
    • 3' UNTRANSLATED REGION
    • AU-RICH ELEMENTS
    • HNRNP A1
    • DECAY
    • DEGRADATION
    • KSRP
    • HUR
    • PHOSPHORYLATION
    • IDENTIFICATION

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