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pubmed-article:12604805pubmed:abstractTextThe hepatitis C virus (HCV) NS5A protein is highly phosphorylated by cellular protein kinases. To study how NS5A might be integrated in cellular kinase signalling, we isolated phosphoproteins from HuH-7 hepatoma cells that specifically interacted with recombinant NS5A protein. Subsequent mass spectrometry identified the adaptor protein amphiphysin II as a novel interaction partner of NS5A. Mutational analysis revealed that complex formation is primarily mediated by a proline-rich region in the C-terminal part of NS5A, which interacts with the amphiphysin II Src homology 3 domain. Importantly, we could further demonstrate specific co-precipitation and cellular co-localization of endogenous amphiphysin II with NS5A in HuH-7 cells carrying a persistently replicating subgenomic HCV replicon. Although the NS5A-amphiphysin II interaction appeared to be dispensable for replication of these HCV RNAs in cell culture, our results indicate that NS5A-amphiphysin II complex formation might be of physiological relevance for the HCV life cycle.lld:pubmed
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pubmed-article:12604805pubmed:articleTitleIdentification and characterization of amphiphysin II as a novel cellular interaction partner of the hepatitis C virus NS5A protein.lld:pubmed
pubmed-article:12604805pubmed:affiliationAxxima Pharmaceuticals AG, Am Klopferspitz 19, 82152 Martinsried, Germany.lld:pubmed
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