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 RIS Download
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