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, p95(vav) is phosphorylated on tyrosine residues, but the kinase regulating its phosphorylation has not been identified to date. Our studies demonstrate that p95(vav) 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, p95(vav) is engaged in IFN-signaling by a direct interaction with the functional type I IFN receptor complex to transduce downstream signals.
Uddin, S., Sweet, M., Colamonici, O. R., Krolewski, J. J., & Platanias, L. C. (1997). The vav proto-oncogene product (p95(vav)) interacts with the Tyk-2 protein tyrosine kinase. FEBS Letters, 403(1), 31–34. https://doi.org/10.1016/S0014-5793(97)00023-9