Giuseppe
Emeritus
Characterization of the interaction of Influenza virus NS1 with Akt. (Biochem Biophys Res Commun., abstract, edited)
[Source: US National Library of Medicine, (LINK). Edited.]
Biochem Biophys Res Commun. 2010 Mar 31. [Epub ahead of print]
Characterization of the interaction of Influenza virus NS1 with Akt.
Matsuda M, Suizu F, Hirata N, Miyazaki T, Obuse C, Noguchi M. - Division of Cancer Biology, Institute for Genetic Medicine, Hokkaido University, Sapporo, Japan.
Avian influenza viruses belong to the genus influenza A virus of the family Orthomyxoviridae. The influenza virus consists of eight segmented minus stranded RNA that encode 11 known proteins. Among the 11 viral proteins, NS1 (Non-structural protein 1, encoded on segment 8) has been implicated in the regulation of several important intracellular functions. In this report, we investigated the functional interaction of NS1 with serine threonine kinase Akt, a core intracellular survival regulator. In co-immunoprecipitation assays and GST pull-down assays, NS1 directly interacted with Akt. The interaction was mediated primarily through the Akt-PH (Pleckstrin Homology) domain and the RNA Binding domain of NS1. NS1 preferentially interacted with phosphorylated Akt, but not with non-phosphorylated Akt. Functionally, the NS1-Akt interaction enhanced Akt kinase activity both in the intra-cellular context and in in vitro Akt kinase assays. Confocal microscopic analysis revealed that phosphorylated Akt interacted with NS1 during the interphase of the cell cycle predominantly within the nucleus. Finally, mass spectrometric analysis demonstrated the position at Thr215 of NS1 protein is primary phosphorylation target site through Akt activation. The results together supported the functional importance of influenza virus NS1 with Akt, a core intracellular survival regulator.
Copyright ? 2010 Elsevier Inc. All rights reserved.
PMID: 20362551 [PubMed - as supplied by publisher]
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[Source: US National Library of Medicine, (LINK). Edited.]
Biochem Biophys Res Commun. 2010 Mar 31. [Epub ahead of print]
Characterization of the interaction of Influenza virus NS1 with Akt.
Matsuda M, Suizu F, Hirata N, Miyazaki T, Obuse C, Noguchi M. - Division of Cancer Biology, Institute for Genetic Medicine, Hokkaido University, Sapporo, Japan.
Avian influenza viruses belong to the genus influenza A virus of the family Orthomyxoviridae. The influenza virus consists of eight segmented minus stranded RNA that encode 11 known proteins. Among the 11 viral proteins, NS1 (Non-structural protein 1, encoded on segment 8) has been implicated in the regulation of several important intracellular functions. In this report, we investigated the functional interaction of NS1 with serine threonine kinase Akt, a core intracellular survival regulator. In co-immunoprecipitation assays and GST pull-down assays, NS1 directly interacted with Akt. The interaction was mediated primarily through the Akt-PH (Pleckstrin Homology) domain and the RNA Binding domain of NS1. NS1 preferentially interacted with phosphorylated Akt, but not with non-phosphorylated Akt. Functionally, the NS1-Akt interaction enhanced Akt kinase activity both in the intra-cellular context and in in vitro Akt kinase assays. Confocal microscopic analysis revealed that phosphorylated Akt interacted with NS1 during the interphase of the cell cycle predominantly within the nucleus. Finally, mass spectrometric analysis demonstrated the position at Thr215 of NS1 protein is primary phosphorylation target site through Akt activation. The results together supported the functional importance of influenza virus NS1 with Akt, a core intracellular survival regulator.
Copyright ? 2010 Elsevier Inc. All rights reserved.
PMID: 20362551 [PubMed - as supplied by publisher]
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