| First Author | Williamson P | Year | 1994 |
| Journal | Leukemia | Volume | 8 Suppl 1 |
| Pages | S186-9 | PubMed ID | 8152289 |
| Mgi Jnum | J:17899 | Mgi Id | MGI:65922 |
| Citation | Williamson P, et al. (1994) The membrane proximal segment of the IL-2 receptor beta-chain acidic region is essential for IL2-dependent protein tyrosine kinase activation. Leukemia 8 Suppl 1:S186-9 |
| abstractText | The signal transduction mechanism of the interleukin-2 receptor (IL-2R) remains largely undefined. The cytosolic domain of the IL-2R beta subunit is known to be essential for coupling to intracellular signaling pathways such as protein tyrosine kinase (PTK) and for control of IL-2 dependent cellular proliferation. A panel of cell lines that express IL-2R beta chains that contain sequential truncation mutations within the cytosolic domain were constructed. These cell lines were used to map the interaction of IL-2R with PTK activation, and the linkage of PTK function to activation of the enzyme phosphatidylinositol-3-kinase (Pl3K). The data show that the amino terminal segment of the acidic region (residues 314-350) within IL-2R beta is a critical site for PTK activation, and that activation of Pl3K is linked to IL-2 dependent tyrosine phosphorylation. |
