14-3-3zeta interacts with the alpha-chain of human interleukin 9 receptor.
Interleukin 9 (IL-9) exerts its pleiotropic effects through the IL-9 receptor (IL-9R) complex, which consists of the IL-9R alpha-chain, which determines the cytokine specificity, and the IL-2 receptor gamma-chain. In the present study we used a modified yeast two-hybrid system to isolate cDNA species encoding proteins that interacted with the ... intracellular domain of the human IL-9R alpha-chain (hIL-9Ralpha). We have identified 14-3-3zeta as an hIL-9Ralpha-interacting protein. We also mapped residues 518-522 (Arg-Ser(519)-Trp-Thr(521)-Phe) in hIL-9Ralpha and helix I of 14-3-3zeta as being important for interaction. Moreover, peptide competition experi-ments suggested that interaction between hIL-9Ralpha and 14-3-3zeta requires the phosphorylation of Ser(519) or Thr(521). This is the first demonstration that 14-3-3 can interact with a non-tyrosine kinase receptor. The interaction between 14-3-3 and IL-9Ralpha but not IL-4Ralpha also suggests a potential role for 14-3-3 in determining cytokine specificity.
Mesh Terms:
14-3-3 Proteins, Amino Acid Sequence, Binding Sites, Humans, Molecular Sequence Data, Phosphorylation, Precipitin Tests, Protein Isoforms, Proteins, Receptors, Interleukin, Receptors, Interleukin-9, Serine, Threonine, Two-Hybrid System Techniques, Tyrosine 3-Monooxygenase
14-3-3 Proteins, Amino Acid Sequence, Binding Sites, Humans, Molecular Sequence Data, Phosphorylation, Precipitin Tests, Protein Isoforms, Proteins, Receptors, Interleukin, Receptors, Interleukin-9, Serine, Threonine, Two-Hybrid System Techniques, Tyrosine 3-Monooxygenase
Biochem. J.
Date: Feb. 01, 2000
PubMed ID: 10642536
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