Physical interaction between interleukin-12 receptor beta 2 subunit and Jak2 tyrosine kinase: Jak2 associates with cytoplasmic membrane-proximal region of interleukin-12 receptor beta 2 via amino-terminus.

IL-12 is a heterodimeric cytokine, composed of p40 and p35 subunits, that exerts its biological effects by binding to specific cell surface receptors. Two human IL-12 receptor proteins, designated IL-12R beta 1 and IL-12R beta 2, have been previously identified. IL-12R beta 2 has box 1 motif, box 2 motif, ...
and three tyrosine residues in its cytoplasmic domain. In response to IL-12, Jak2 and Tyk2, family members of Janus family protein tyrosine kinases, are phosphorylated in PHA-activated T lymphocytes. The present study demonstrates that Jak2 binds to the cytoplasmic membrane-proximal region of IL-12R beta 2, and box 2 motif and tyrosine residues in the cytoplasmic domain were not required for binding. The amino-terminus of Jak2 is necessary for association with IL-12R beta 2.
Mesh Terms:
Amino Acid Substitution, Animals, COS Cells, Cell Membrane, Cytoplasm, Escherichia coli, Janus Kinase 2, Phosphorylation, Phosphotyrosine, Precipitin Tests, Protein Binding, Protein-Tyrosine Kinases, Proteins, Proto-Oncogene Proteins, Receptor Protein-Tyrosine Kinases, Receptor, EphB4, Receptors, Eph Family, Receptors, Interleukin, Receptors, Interleukin-12, Recombinant Fusion Proteins, Sequence Deletion, Transfection, Tyrosine
Biochem. Biophys. Res. Commun.
Date: Apr. 13, 1999
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