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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
Pt 3
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pubmed:dateCreated |
2003-2-26
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pubmed:abstractText |
The 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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/MAP Kinase Kinase Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/NS-5 protein, hepatitis C virus,
http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proline,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Replicase,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Nonstructural Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/amphiphysin,
http://linkedlifedata.com/resource/pubmed/chemical/mitogen-activated protein kinase...
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0022-1317
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pubmed:author |
pubmed-author:BartenschlagerRalfR,
pubmed-author:BlenckeStephanieS,
pubmed-author:CottenMattM,
pubmed-author:DaubHenrikH,
pubmed-author:HergetThomasT,
pubmed-author:KriegerNicoleN,
pubmed-author:KurtenbachAlexanderA,
pubmed-author:MorbitzerMonikaM,
pubmed-author:ObertSabineS,
pubmed-author:SalassidisKostasK,
pubmed-author:StrandDennisD,
pubmed-author:WissingJosefJ,
pubmed-author:ZechBirgitB
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pubmed:issnType |
Print
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pubmed:volume |
84
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
555-60
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:12604805-Cytoplasm,
pubmed-meshheading:12604805-Fluorescent Antibody Technique, Indirect,
pubmed-meshheading:12604805-Hepacivirus,
pubmed-meshheading:12604805-Humans,
pubmed-meshheading:12604805-Immunoblotting,
pubmed-meshheading:12604805-Leucine Zippers,
pubmed-meshheading:12604805-MAP Kinase Kinase Kinases,
pubmed-meshheading:12604805-Mutation,
pubmed-meshheading:12604805-Nerve Tissue Proteins,
pubmed-meshheading:12604805-Proline,
pubmed-meshheading:12604805-Protein Binding,
pubmed-meshheading:12604805-Protein-Serine-Threonine Kinases,
pubmed-meshheading:12604805-RNA Replicase,
pubmed-meshheading:12604805-Recombinant Proteins,
pubmed-meshheading:12604805-Replicon,
pubmed-meshheading:12604805-Tumor Cells, Cultured,
pubmed-meshheading:12604805-Viral Nonstructural Proteins,
pubmed-meshheading:12604805-Virus Replication
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pubmed:year |
2003
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pubmed:articleTitle |
Identification and characterization of amphiphysin II as a novel cellular interaction partner of the hepatitis C virus NS5A protein.
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pubmed:affiliation |
Axxima Pharmaceuticals AG, Am Klopferspitz 19, 82152 Martinsried, Germany.
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pubmed:publicationType |
Journal Article
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