SH2-dependent association of phosphatidylinositol 3'-kinase 85-kDa regulatory subunit with the interleukin-2 receptor beta chain
| Autor: | K E, Truitt, G B, Mills, C W, Turck, J B, Imboden |
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| Rok vydání: | 1994 |
| Předmět: |
Binding Sites
Molecular Sequence Data Proto-Oncogene Proteins pp60(c-src) Receptors Interleukin-2 Precipitin Tests Peptide Fragments Kinetics Phosphatidylinositol 3-Kinases Phosphotransferases (Alcohol Group Acceptor) Humans Tyrosine Receptors Platelet-Derived Growth Factor Amino Acid Sequence Phosphorylation Oligopeptides Signal Transduction |
| Zdroj: | The Journal of biological chemistry. 269(8) |
| ISSN: | 0021-9258 |
| Popis: | Interleukin-2 (IL-2) signaling results in tyrosine phosphorylation of the 75-kDa IL-2 receptor (IL-2R) beta chain and the activation of phosphatidylinositol 3'-kinase (PI3-K). Herein, we demonstrate that the 85-kDa (p85) regulatory subunit of PI3-K physically associates with the tyrosine-phosphorylated IL-2R beta chain. A fusion protein containing both the amino- and the carboxyl-terminal src homology 2 domains of p85 precipitates an 80-kDa tyrosine-phosphorylated protein (pp80) from the lysates of IL-2-stimulated, but not unstimulated, human T lymphoblasts. Preclearing studies and immunoblotting with an antiserum to the IL-2R beta chain demonstrates that pp80 represents a portion of the IL-2R beta chain pool. A tyrosine-phosphorylated oligopeptide corresponding to tyrosine 392 of the IL-2R beta chain partially inhibits binding of the IL-2R beta chain by p85 fusion protein, raising the possibility that this residue plays a role in the interaction of PI3-K with the receptor. |
| Databáze: | OpenAIRE |
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