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Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1.

In mammalian cells, splice junctions play a dual role in mRNA quality control: They mediate selective nuclear export of mature mRNA and they serve as a mark for mRNA surveillance, which subjects aberrant mRNAs with premature termination codons to nonsense-mediated decay (NMD). Here, we demonstrate that the protein RNPS1, a component of the postsplicing complex that is deposited 5' to exon-exon junctions, interacts with the evolutionarily conserved human Upf complex, a central component of NMD. Significantly, RNPS1 triggers NMD when tethered to the 3' untranslated region of beta-globin mRNA, demonstrating its role as a subunit of the postsplicing complex directly involved in mRNA surveillance.

Pubmed ID: 11546874


  • Lykke-Andersen J
  • Shu MD
  • Steitz JA


Science (New York, N.Y.)

Publication Data

September 7, 2001

Associated Grants

  • Agency: NCI NIH HHS, Id: CA 16038

Mesh Terms

  • 3' Untranslated Regions
  • Animals
  • Cell Line
  • DNA-Binding Proteins
  • Exons
  • Fungal Proteins
  • Globins
  • HeLa Cells
  • Humans
  • Macromolecular Substances
  • Mice
  • Models, Biological
  • Precipitin Tests
  • Protein Binding
  • RNA Helicases
  • RNA Splicing
  • RNA, Messenger
  • RNA-Binding Proteins
  • Recombinant Fusion Proteins
  • Ribonucleoproteins
  • Saccharomyces cerevisiae Proteins
  • Trans-Activators
  • Transfection