The vav proto-oncogene product (p95(vav)) interacts with the Tyk-2 protein tyrosine kinase

Shahab Uddin; Michelle Sweet; Oscar R. Colamonici; John J. Krolewski; Leonidas C. Platanias

doi:10.1016/S0014-5793(97)00023-9

The vav proto-oncogene product (p95(vav)) interacts with the Tyk-2 protein tyrosine kinase

Shahab Uddin, Michelle Sweet, Oscar R. Colamonici, John J. Krolewski, Leonidas C. Platanias^*

^*Corresponding author for this work

Medicine, Hematology Oncology Division

Research output: Contribution to journal › Article › peer-review

31 Scopus citations

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, 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.

Original language	English (US)
Pages (from-to)	31-34
Number of pages	4
Journal	FEBS Letters
Volume	403
Issue number	1
DOIs	https://doi.org/10.1016/S0014-5793(97)00023-9
State	Published - Feb 10 1997

Keywords

Interferon signaling
Jak kinase
vav Proto-oncogene

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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10.1016/S0014-5793(97)00023-9

Cite this

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title = "The vav proto-oncogene product (p95(vav)) interacts with the Tyk-2 protein tyrosine kinase",

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, 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.",

keywords = "Interferon signaling, Jak kinase, vav Proto-oncogene",

author = "Shahab Uddin and Michelle Sweet and Colamonici, {Oscar R.} and Krolewski, {John J.} and Platanias, {Leonidas C.}",

note = "Funding Information: This work was supported by grant CA73381 from the National Institutes of Health (to L.C.P.). ",

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AU - Sweet, Michelle

AU - Colamonici, Oscar R.

AU - Krolewski, John J.

AU - Platanias, Leonidas C.

N1 - Funding Information: This work was supported by grant CA73381 from the National Institutes of Health (to L.C.P.).

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N2 - 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.

AB - 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.

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The vav proto-oncogene product (p95(vav)) interacts with the Tyk-2 protein tyrosine kinase

Abstract

Keywords

ASJC Scopus subject areas

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