The protein Mago provides a link between splicing and mRNA localization

EMBO Rep. 2001 Dec;2(12):1119-24. doi: 10.1093/embo-reports/kve245. Epub 2001 Nov 21.

Abstract

The proteins Mago and Y14 are evolutionarily conserved binding partners. Y14 is a component of the exon-exon junction complex (EJC), deposited by the spliceosome upstream of messenger RNA (mRNA) exon-exon junctions. The EJC is implicated in post-splicing events such as mRNA nuclear export and nonsense-mediated mRNA decay. Drosophila Mago is essential for the localization of oskar mRNA to the posterior pole of the oocyte, but the functional role of Mago in other species is unknown. We show that Mago is a bona fide component of the EJC. Like Y14, Mago escorts spliced mRNAs to the cytoplasm, providing a direct functional link between splicing and the downstream process of mRNA localization. Mago/Y14 heterodimers are essential in cultured Drosophila cells. Taken together, these results suggest that, in addition to its specialized function in mRNA localization, Mago plays an essential role in other steps of mRNA metabolism.

MeSH terms

  • Animals
  • Biological Transport
  • Cell Division
  • Cell Line
  • Cell Nucleus Structures / metabolism
  • Cytoplasm / metabolism
  • DNA / genetics
  • Dimerization
  • Drosophila / cytology
  • Drosophila / genetics
  • Drosophila / metabolism
  • Drosophila Proteins*
  • Evolution, Molecular
  • Exons / genetics
  • HeLa Cells
  • Humans
  • Male
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Polymerase Chain Reaction
  • Protein Binding
  • RNA Splicing / genetics*
  • RNA, Messenger / chemistry
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism*
  • RNA-Binding Proteins / genetics
  • RNA-Binding Proteins / metabolism
  • Testis
  • Transfection
  • Xenopus

Substances

  • Drosophila Proteins
  • MAGOH protein, human
  • Mago protein, Drosophila
  • Nuclear Proteins
  • RBM8A protein, human
  • RNA, Messenger
  • RNA-Binding Proteins
  • DNA