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.
Pubmed ID: 10198225 RIS Download
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