TY - JOUR
T1 - Non-structural protein 1 of influenza viruses inhibits rapid mRNA degradation mediated by double-stranded RNA-binding protein, staufen1
AU - Cho, Hana
AU - Ahn, Sang Ho
AU - Kim, Kyoung Mi
AU - Kim, Yoon Ki
N1 - Funding Information:
We thank Lynne E. Maquat for providing NMD reporter plasmids and α-Upf1 antibody, Luc DesGroseillers for plasmid expressing Stau1 55 -HA 3 , Jens Lykke-Andersen for tethering reporter plasmids, and Kyung Hyun Kim for plasmid expressing NS1. This work was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education, Science and Technology (2012R1A2A1A01002469) and by the Korea Healthcare Technology R&D Project (A103001), Ministry for Health, Welfare and Family Affairs , Republic of Korea.
PY - 2013/7/11
Y1 - 2013/7/11
N2 - 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. 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).
AB - 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. 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).
KW - Influenza virus
KW - NS1
KW - Staufen1
KW - Staufen1-mediated mRNA decay (SMD)
UR - http://www.scopus.com/inward/record.url?scp=84879688343&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2013.05.029
DO - 10.1016/j.febslet.2013.05.029
M3 - Article
C2 - 23722113
AN - SCOPUS:84879688343
VL - 587
SP - 2118
EP - 2124
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 14
ER -