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

@article{Bono2004MolecularII,
  title={Molecular insights into the interaction of PYM with the Mago-Y14 core of the exon junction complex.},
  author={Fulvia Bono and Judith Ebert and Leonie Unterholzner and Thomas G{\"u}ttler and Elisa Izaurralde and Elena Conti},
  journal={EMBO reports},
  year={2004},
  volume={5 3},
  pages={304-10}
}
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… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 36 extracted citations

References

Publications referenced by this paper.
Showing 1-10 of 25 references

Genome-wide analysis of nuclear export pathways in Drosophila

  • A Herold, L Teixera, E Izaurralde
  • EMBO J
  • 2003
1 Excerpt

Similar Papers

Loading similar papers…