Abstract
The c-cbl proto-oncogene product (p120cbl) forms a stable complex with the Tyk-2 protein tyrosine kinase in various human cell lines of diverse hematopoietic origin. In U-266 myeloma and 293T embryonic kidney cells, p120cbl is rapidly phosphorylated on tyrosine in an IFN alpha-dependent manner. p120cbl also acts as a specific substrate for the Tyk-2-associated SHP-1 phosphatase in vitro, suggesting that this phosphatase plays a regulatory role on the phosphorylation of the protein. These data provide evidence that p120cbl interacts with the functional Type I IFN receptor complex, and suggest its involvement in IFN alpha signaling.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Cell Line
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Humans
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Interferon-alpha / metabolism
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Intracellular Signaling Peptides and Proteins
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Phosphorylation
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Protein Tyrosine Phosphatase, Non-Receptor Type 11
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Protein Tyrosine Phosphatase, Non-Receptor Type 6
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Protein Tyrosine Phosphatases / metabolism
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Protein-Tyrosine Kinases / metabolism*
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Proteins / metabolism*
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Proto-Oncogene Mas
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Proto-Oncogene Proteins / metabolism*
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Proto-Oncogene Proteins c-cbl
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Receptor, Interferon alpha-beta
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Receptors, Interferon / metabolism
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Signal Transduction
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Substrate Specificity
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TYK2 Kinase
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Ubiquitin-Protein Ligases*
Substances
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Interferon-alpha
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Intracellular Signaling Peptides and Proteins
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MAS1 protein, human
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Proteins
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Proto-Oncogene Mas
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Proto-Oncogene Proteins
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Receptors, Interferon
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Receptor, Interferon alpha-beta
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Proto-Oncogene Proteins c-cbl
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Ubiquitin-Protein Ligases
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Protein-Tyrosine Kinases
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TYK2 Kinase
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TYK2 protein, human
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PTPN11 protein, human
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PTPN6 protein, human
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Protein Tyrosine Phosphatase, Non-Receptor Type 11
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Protein Tyrosine Phosphatase, Non-Receptor Type 6
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Protein Tyrosine Phosphatases
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CBL protein, human