Abstract
Interleukin-2 (IL-2) is a polypeptide growth factor which stimulates the proliferation and differentiation of T lymphocytes1,2. The receptor for IL-2 is expressed on activated T lymphocytes, cloned IL-2 dependent cells and several other cell types. Analysis of the primary structure and of immune-precipitated receptor suggests that this molecule has no intrinsic signal transduction function, unlike other growth factors. IL-2 interaction with a high affinity receptor3 has been shown, however, to activate the calcium/phos-pholipid-dependent protein kinase C (PK-C)4,5 presumably via phosphoinositide hydrolysis. Members of a family of closely related guanine nucleotide binding proteins (G proteins) regulate a diverse group of metabolic events6,7. Two of them, Gs and Gi, stimulate and inhibit adenylate cyclase activity respectively8–11, and other G proteins are involved in diverse signal transduction systems12–16. Another member, Go, has no known function and activation of phospholipase C has been attributed to the action of an unidentified G protein, GP17–19. Since it has been observed that IL-2 inhibits the catalytic activity of adenylate cyclase and that agents such as PGE2 which stimulate adenylate cyclase activity inhibit the lymphoproliferative response to IL-220, association of GTP binding proteins with IL-2 signal transduction was investigated. In this report we describe for the first time the participation of a GTP binding protein in the action of a polypeptide growth factor, interleukin-2.
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Evans, S., Beckner, S. & Farrar, W. Stimulation of specific GTP binding and hydrolysis activities in lymphocyte membrane by interleukin-2. Nature 325, 166–168 (1987). https://doi.org/10.1038/325166a0
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DOI: https://doi.org/10.1038/325166a0
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