Uddin S, Sweet M, Colamonici O R, Krolewski J J, Platanias L C
Department of Medicine, University of Illinois at Chicago, 60607, USA.
FEBS Lett. 1997 Feb 10;403(1):31-4. doi: 10.1016/s0014-5793(97)00023-9.
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.
