Magoh, a human homolog of Drosophila mago nashi protein, is a component of the splicing-dependent exon-exon junction complex

Naoyuki Kataoka, Michael D. Diem, V. Narry Kim, Jeongsik Yong, Gideon Dreyfuss

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165 Scopus citations

Abstract

The RNA-binding protein Y14 binds preferentially to mRNAs produced by splicing and is a component of a multiprotein complex that assembles ∼20 nucleotides upstream of exon-exon junctions. This complex probably has important functions in post-splicing events including nuclear export and nonsense-mediated decay of mRNA. We show that Y14 binds to two previously reported components, Aly/REF and RNPS1, and to the mRNA export factor TAP. Moreover, we identified magoh, a human homolog of the Drosophila mago nashi gene product, as a novel component of the complex. Magoh binds avidly and directly to Y14 and TAP, but not to other known components of the complex, and is found in Y14-containing mRNPs in vivo. Importantly, magoh also binds to mRNAs produced by splicing upstream (∼20 nucleotides) of exonexon junctions and its binding to mRNA persists after export. These experiments thus reveal specific protein-protein interactions among the proteins of the splicing-dependent mRNP complex and suggest an important role for the highly evolutionarily conserved magoh protein in this complex.

Original languageEnglish (US)
Pages (from-to)6424-6433
Number of pages10
JournalEMBO Journal
Volume20
Issue number22
DOIs
StatePublished - Nov 15 2001

Keywords

  • Exon-exon junction complex
  • Mago nashi
  • Magoh
  • Splicing
  • Y14

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