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Role of the nonsense-mediated decay factor hUpf3 in the splicing-dependent exon-exon junction complex.

Nonsense-mediated messenger RNA (mRNA) decay, or NMD, is a critical process of selective degradation of mRNAs that contain premature stop codons. NMD depends on both pre-mRNA splicing and translation, and it requires recognition of the position of stop codons relative to exon-exon junctions. A key factor in NMD is hUpf3, a mostly nuclear protein that shuttles between the nucleus and cytoplasm and interacts specifically with spliced mRNAs. We found that hUpf3 interacts with Y14, a component of post-splicing mRNA-protein (mRNP) complexes, and that hUpf3 is enriched in Y14-containing mRNP complexes. The mRNA export factors Aly/REF and TAP are also associated with nuclear hUpf3, indicating that hUpf3 is in mRNP complexes that are poised for nuclear export. Like Y14 and Aly/REF, hUpf3 binds to spliced mRNAs specifically ( approximately 20 nucleotides) upstream of exon-exon junctions. The splicing-dependent binding of hUpf3 to mRNAs before export, as part of the complex that assembles near exon-exon junctions, allows it to serve as a link between splicing and NMD in the cytoplasm.

Pubmed ID: 11546873


  • Kim VN
  • Kataoka N
  • Dreyfuss G


Science (New York, N.Y.)

Publication Data

September 7, 2001

Associated Grants

  • Agency: NIGMS NIH HHS, Id: 5 R01 GM37125.14

Mesh Terms

  • 3' Untranslated Regions
  • Active Transport, Cell Nucleus
  • Cell Line
  • Codon, Nonsense
  • DNA-Binding Proteins
  • Exons
  • Fungal Proteins
  • Globins
  • Humans
  • Macromolecular Substances
  • Models, Biological
  • Precipitin Tests
  • Protein Binding
  • RNA Splicing
  • RNA, Messenger
  • RNA-Binding Proteins
  • Recombinant Fusion Proteins
  • Ribonucleoproteins
  • Saccharomyces cerevisiae Proteins
  • Substrate Specificity