Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex

Fulvia Bono, Judith Ebert, Leonie Unterholzner, Thomas Güttler, Elisa Izaurralde, Elena Conti

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    74 Citations (Scopus)

    Abstract

    The exon junction complex (EJC) is deposited on mRNAs as a consequence of splicing and influences postsplicing mRNA metabolism. The Mago-Y14 heterodimer is a core component of the EJC. Recently, the protein PYM has been identified as an interacting partner of Mago-Y14. Here we show that PYM is a cytoplasmic RNA-binding protein that is excluded from the nucleus by Crm1. PYM interacts directly with Mago-Y14 by means of its N-terminal domain. The crystal structure of the Drosophila ternary complex at 1.9 A resolution reveals that PYM binds Mago and Y14 simultaneously, capping their heterodimerization interface at conserved surface residues. Formation of this ternary complex is also observed with the human proteins. Mago residues involved in the interaction with PYM have been implicated in nonsense-mediated mRNA decay (NMD). Consistently, human PYM is active in NMD tethering assays. Together, these data suggest a role for PYM in NMD.
    Original languageEnglish
    Pages (from-to)304-10
    Number of pages7
    JournalEMBO Reports
    Volume5
    Issue number3
    DOIs
    Publication statusPublished - Mar 2004

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    Bono, F., Ebert, J., Unterholzner, L., Güttler, T., Izaurralde, E., & Conti, E. (2004). Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex. EMBO Reports, 5(3), 304-10. https://doi.org/10.1038/sj.embor.7400091