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Non-structural protein 1 of influenza viruses inhibits rapid mRNA degradation mediated by double-stranded RNA-binding protein, staufen1

Authors
Cho, HanaAhn, Sang HoKim, Kyoung MiKim, Yoon Ki
Issue Date
11-7월-2013
Publisher
WILEY
Keywords
Influenza virus; NS1; Staufen1; Staufen1-mediated mRNA decay (SMD)
Citation
FEBS LETTERS, v.587, no.14, pp.2118 - 2124
Indexed
SCIE
SCOPUS
Journal Title
FEBS LETTERS
Volume
587
Number
14
Start Page
2118
End Page
2124
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/102714
DOI
10.1016/j.febslet.2013.05.029
ISSN
0014-5793
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-mediated-mRNA decay (NMD). The regulation of SMD efficiency by NS1 may contribute to building a more favorable cellular environment for viral replication. Structured summary of protein interactions: STAU1-55 physically interacts with UPF1 by anti tag-coimmunoprecipitation (View interaction) NS1 physically interacts with STAU1-55 by anti tag-coimmunoprecipitation (View interaction) (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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