Tyrosine phosphorylation of measles virus P-phosphoprotein in persistently infected neuroblastoma cells

• Published in: Virus genes 1996, Vol.13 (3), p.203-210
• Main Authors: Ofir, R, Weinstein, Y, Bazarsky, E, Blagerman, S, Wolfson, M, Hunter, T, Rager-Zisman, B
• Format: Article
• Language: English
• Subjects: Animals; measles virus; Measles virus - metabolism; Mice; Neuroblastoma; Phosphoproteins - genetics; Phosphoproteins - metabolism; Phosphorylation; Protein Binding; Protein-Tyrosine Kinases - metabolism; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; Serine - metabolism; src-Family Kinases; Threonine - metabolism; Tumor Cells, Cultured; Tyrosine - metabolism; Viral Proteins - genetics; Viral Proteins - metabolism; Virus Latency
• ISSN: 0920-8569; 1572-994X
• DOI: 10.1007/BF00366980

Replication and encapsidation of measles virus (MV) requires the interaction between the nuclear protein (N) and the phosphoprotein (P). It is known that both proteins are phosphorylated on serine and threonine residues. Recently we have shown that N is phosphorylated on tyrosine in persistently-infected mouse neuroblastoma cells (NS20Y/MS). Here, we show that P in NS20Y/MS is also phosphorylated on tyrosine. To investigate whether cellular tyrosine kinases can bind and phosphorylate P, a solid phase kinase assay was employed. We show that bacterially-expressed MV P fragments, were phosphorylated on tyrosine by purified mouse c-Src protein-tyrosine kinase and when mixed with uninfected neuroblastoma cell (NS20Y) extracts, these P fragments were phosphorylated on tyrosine in addition to serine and threonine. These results imply that MV P is a substrate for tyrosine phosphorylation by cellular tyrosine kinase(s).