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*
Immunology Program, Cornell University Graduate School of Medical Sciences, and Department of Medicine, Division of Immunology, Cornell University Medical College, New York, NY 10021;
Laboratory of Allergic Diseases, National Institute of Allergy and Infectious Diseases/National Institutes of Health, Rockville MD 20852; and
Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases/National Institutes of Health, Bethesda, MD 20892
The newly recognized regulators of G protein signaling (RGS)
attenuate heterotrimeric G protein signaling pathways. We have cloned
an IL-2-induced gene from human T cells, cytokine-responsive gene 1,
which encodes a member of the RGS family, RGS16. The RGS16 protein
binds Gi
and Gq
proteins present in T
cells, and inhibits Gi- and Gq-mediated
signaling pathways. By comparison, the mitogen-induced RGS2 inhibits
Gq but not Gi signaling. Moreover, the two RGS
genes exhibit marked differences in expression patterns. The
IL-2-induced expression of the RGS16 gene in T cells is suppressed by
elevated cAMP, whereas the RGS2 gene shows a reciprocal pattern of
regulation by these stimuli. Because the mitogen and cytokine receptors
that trigger expression of RGS2 and RGS16 in T cells do not activate
heterotrimeric G proteins, these RGS proteins and the G proteins that
they regulate may play a heretofore unrecognized role in T cell
functional responses to Ag and cytokine
activation.
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