title: Non-structural protein 1 of influenza viruses inhibits rapid mRNA degradation mediated by double-stranded RNA-binding protein, staufen1.
abstract: Although non-structural protein 1 (NS1) of influenza viruses is not essential for virulence, this protein is involved in host-virus interactions, viral replication, and translation. In particular, NS1 is known to interact with the host protein, staufen1 (Stau1). This interaction is important for efficient viral replication. However, the underlying molecular mechanism by which NS1 influences the viral life cycle remains obscure. Here, we show using immunoprecipitation and artificial tethering that the N-terminus of NS1, NS1(1-73), interacts with Stau1, blocks the Stau1-Upf1 interaction, and consequently inhibits the efficiency of Stau1-mediated mRNA decay (SMD), but not nonsense-mediatedmRNA decay (NMD). The regulation of SMD efficiency by NS1 may contribute to building a more favorable cellular environment for viral replication.
authors.affiliation: School of Life Sciences and Biotechnology, Korea University, Seoul 136-701, Republic of Korea.
authors.forename: Hana
authors.initials: H
authors.lastname: Cho
authors.forename: Sang Ho
authors.initials: SH
authors.lastname: Ahn
authors.forename: Kyoung Mi
authors.initials: KM
authors.lastname: Kim
authors.forename: Yoon Ki
authors.initials: YK
authors.lastname: Kim
mesh_terms: D048868:Adaptor Proteins, Signal Transducing / Q000235:genetics / Q000378:metabolism; D003598:Cytoskeletal Proteins / Q000737:chemistry / Q000378:metabolism*; D015870:Gene Expression; D005786:Gene Expression Regulation; D057809:HEK293 Cells; D006367:HeLa Cells; D054884:Host-Pathogen Interactions; D006801:Humans; D051741:Kruppel-Like Transcription Factors / Q000235:genetics / Q000378:metabolism; D059365:Nonsense Mediated mRNA Decay; D009975:Orthomyxoviridae / Q000502:physiology*; D011485:Protein Binding; D054730:Protein Interaction Domains and Motifs; D020365:RNA Helicases; D020871:RNA Stability; D012330:RNA, Double-Stranded / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism*; D016601:RNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D020395:Receptors, Interleukin-7 / Q000235:genetics / Q000378:metabolism; D015534:Trans-Activators / Q000378:metabolism; D017361:Viral Nonstructural Proteins / Q000737:chemistry / Q000378:metabolism*; D014779:Virus Replication
chemical_list: D048868:Adaptor Proteins, Signal Transducing; C554642:COMMD7 protein, human; D003598:Cytoskeletal Proteins; C096161:KLF2 protein, human; D051741:Kruppel-Like Transcription Factors; D012330:RNA, Double-Stranded; D012333:RNA, Messenger; D016601:RNA-Binding Proteins; D020395:Receptors, Interleukin-7; C492185:STAU1 protein, human; D015534:Trans-Activators; D017361:Viral Nonstructural Proteins; D020365:RNA Helicases; C101828:UPF1 protein, human