herbimycin and Multiple-Myeloma

The vav proto-oncogene product participates in the signaling pathways activated by various cell-surface receptors, including the type I IFN receptor. During engagement of the type I IFN receptor, p95vav is phosphorylated on tyrosine residues, but the kinase regulating its phosphorylation has not been identified to date. Our studies demonstrate that p95vav forms a stable complex with the IFN-receptor-associated Tyk-2 kinase in vivo, and strongly suggest that this kinase regulates its phosphorylation on tyrosine. Thus, p95vav is engaged in IFN-signaling by a direct interaction with the functional type I IFN receptor complex to transduce downstream signals.

Topics: Benzoquinones; Cell Cycle Proteins; Enzyme Inhibitors; Genistein; Humans; Interferon-alpha; Isoflavones; Lactams, Macrocyclic; Multiple Myeloma; Phosphorylation; Precipitin Tests; Protein-Tyrosine Kinases; Proteins; Proto-Oncogene Mas; Proto-Oncogene Proteins; Proto-Oncogene Proteins c-vav; Quinones; Rifabutin; Staurosporine; Tumor Cells, Cultured; TYK2 Kinase; Tyrosine