CBP80 promotes interaction of Upf1 with Upf2 during nonsense-mediated mRNA decay in mammalian cells

Nao Hosoda, Yoon Ki Kim, Fabrice Lejeune, Lynne E. Maquat

Research output: Contribution to journalArticle

99 Citations (Scopus)

Abstract

In mammalian cells, nonsense-mediated messenger RNA decay (NMD) targets newly synthesized nonsense-containing mRNA bound by the cap-binding-protein heterodimer CBP80-CBP20 and at least one exon-junction complex (EJC). An EJC includes the NMD factors Upf3 or Upf3X and Upf2, and Upf2 recruits Upf1. Once this pioneer translation initiation complex is remodeled so that CBP80-CBP20 is replaced by eukaryotic initiation factor 4E, the mRNA is no longer detectably targeted for NMD. Here, we provide evidence that CBP80 augments the efficiency of NMD but not of Staufen1 (Stau1)-mediated mRNA decay (SMD). SMD depends on the recruitment of Upf1 by the RNA-binding protein Stau1 but does not depend on the other Upf proteins. We find that CBP80 interacts with Upf1 and promotes the interaction of Upf1 with Upf2 but not with Stau1.

Original languageEnglish
Pages (from-to)893-901
Number of pages9
JournalNature Structural and Molecular Biology
Volume12
Issue number10
DOIs
Publication statusPublished - 2005 Oct 1

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Nonsense Mediated mRNA Decay
RNA Stability
Messenger RNA
Exons
RNA Cap-Binding Proteins
Eukaryotic Initiation Factor-4E
RNA-Binding Proteins

ASJC Scopus subject areas

  • Molecular Biology
  • Structural Biology

Cite this

CBP80 promotes interaction of Upf1 with Upf2 during nonsense-mediated mRNA decay in mammalian cells. / Hosoda, Nao; Kim, Yoon Ki; Lejeune, Fabrice; Maquat, Lynne E.

In: Nature Structural and Molecular Biology, Vol. 12, No. 10, 01.10.2005, p. 893-901.

Research output: Contribution to journalArticle

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