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• W1505648210 endingPage "601" @default.
• W1505648210 startingPage "587" @default.
• W1505648210 abstract "The vacuolar (H+)-ATPases (V-ATPases) facilitate the release of influenza A virus (IAV) genome into the cytoplasm by acidifying the endosomal interior. The regulation of V-ATPases by signalling pathways has been demonstrated in various model systems. However, little is known about signalling-regulated V-ATPase activation during IAV infection. Here we show that V-ATPase activity is elevated during infection of cell monolayers with IAV, as measured by intracellular pH change, via a mechanism mediated by extracellular signal-regulated kinase (ERK) and phosphatidylinositol 3-kinase (PI3K). Inhibition of IAV-induced early activation of these kinases reduced V-ATPase activity and the acidification of intracellular compartments in infected cells. IAV-activated ERK and PI3K appear to interact directly, and they colocalize with the E subunit of V-ATPase V1 domain. Further, siRNAs targeting the E2 subunit isoform significantly reduced virus titres. Interestingly, suppression of PI3K early activation, but not that of ERK or V-ATPase, negatively affected virus internalization, suggesting the involvement of the pathway in earlier, V-ATPase-independent infection-promoting events. Cell treatment with a V-ATPase-specific inhibitor impaired the nuclear localization of incoming viral ribonucleoproteins, inhibiting replication/transcription of viral RNAs. These findings highlight the importance of IAV-induced ERK and PI3K early activation as signalling mediators in V-ATPase-stimulated endosomal acidification required for fusion." @default.
• W1505648210 created "2016-06-24" @default.
• W1505648210 creator A5002367868 @default.
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• W1505648210 date "2010-12-29" @default.
• W1505648210 modified "2023-10-16" @default.
• W1505648210 title "Influenza A virus-induced early activation of ERK and PI3K mediates V-ATPase-dependent intracellular pH change required for fusion" @default.
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• W1505648210 doi "https://doi.org/10.1111/j.1462-5822.2010.01556.x" @default.
• W1505648210 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3552532" @default.
• W1505648210 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21129142" @default.
• W1505648210 hasPublicationYear "2010" @default.
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