Abstract
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.
Publication types
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Benzoquinones
-
Cell Cycle Proteins*
-
Enzyme Inhibitors / pharmacology
-
Genistein
-
Humans
-
Interferon-alpha / metabolism
-
Interferon-alpha / pharmacology
-
Isoflavones / pharmacology
-
Lactams, Macrocyclic
-
Multiple Myeloma / drug therapy
-
Multiple Myeloma / metabolism
-
Multiple Myeloma / pathology
-
Phosphorylation
-
Precipitin Tests
-
Protein-Tyrosine Kinases*
-
Proteins / antagonists & inhibitors
-
Proteins / metabolism*
-
Proto-Oncogene Mas
-
Proto-Oncogene Proteins / genetics
-
Proto-Oncogene Proteins / immunology
-
Proto-Oncogene Proteins / metabolism*
-
Proto-Oncogene Proteins c-vav
-
Quinones / pharmacology
-
Rifabutin / analogs & derivatives
-
Staurosporine / pharmacology
-
TYK2 Kinase
-
Tumor Cells, Cultured
-
Tyrosine / metabolism
Substances
-
Benzoquinones
-
Cell Cycle Proteins
-
Enzyme Inhibitors
-
Interferon-alpha
-
Isoflavones
-
Lactams, Macrocyclic
-
MAS1 protein, human
-
Proteins
-
Proto-Oncogene Mas
-
Proto-Oncogene Proteins
-
Proto-Oncogene Proteins c-vav
-
Quinones
-
VAV1 protein, human
-
Rifabutin
-
Tyrosine
-
herbimycin
-
Genistein
-
Protein-Tyrosine Kinases
-
TYK2 Kinase
-
TYK2 protein, human
-
Staurosporine