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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

Authors

  • Yamamoto K
  • Shibata F
  • Miura O
  • Kamiyama R
  • Hirosawa S
  • Miyasaka N

Journal

Biochemical and biophysical research communications

Publication Data

April 13, 1999

Associated Grants

None

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