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The membrane proximal segment of the IL-2 receptor beta-chain acidic region is essential for IL2-dependent protein tyrosine kinase activation

Williamson, P.; Merida, I.; Greene, W.C.; Gaulton, G.

Leukemia 8(Suppl): S186-S189

1994

ISSN/ISBN: 0887-6924
PMID: 8152289
Document Number: 428424
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 (PI3K). 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 PI3K is linked to IL-2 dependent tyrosine phosphorylation.

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