Document Actions
Communication of the position of exon-ex ... machinery by the protein RNPS1
Communication of the position of exon-exon junctions to the mRNA surveillance machinery by the protein RNPS1.
25
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.
Lykke-Andersen J, Shu MD, Steitz JA
Science (New York, N.Y.)
2001-09-07 00:00
293
5536
1836-9
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,3' Untranslated Regions,DNA-Binding Proteins,Fungal Proteins,Macromolecular Substances,RNA, Messenger,RNA-Binding Proteins,RNPS1 protein, human,Recombinant Fusion Proteins,Rent1 protein, mouse,Ribonucleoproteins,Rnps1 protein, mouse,Saccharomyces cerevisiae Proteins,Trans-Activators,UPF1 protein, human,UPF3 protein, S cerevisiae,Globins,RNA Helicases
Howard Hughes Medical Institute, Molecular Biochemistry and Biophysics, Yale University School of Medicine, 295 Congress Avenue, New Haven, CT 06536, USA
Science
NCI CA 16038
0036-8075
10.1126/science.1062786
293/5536/1836
803
True
11546874
