Poster: Signaling, cell-to-cell
Abs #
425: Role of a Seven-transmembrane RGS Protein in Sugar Signaling in Arabidopsis
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Presenter: |
Jones, Alan M., alan_jones@unc.edu |
Authors | Jones, Alan M. (A) Chen, Jin-Gui (A) Huang, Jirong (A) | | Affiliations: |
(A): Dept. of Biology, University of North Carolina at Chapel Hill
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Regulators of G Signaling (RGS) proteins accelerate the intrinsic GTPase activity of the alpha subunit of heterotrimeric G proteins and thereby desensitize cells to signals that are coupled by G proteins. Arabidopsis contains a single RGS1 protein. This RGS (AtRGS1) contains a seven-transmembrane domain at its amino-terminal half and a functional RGS domain at its cytosolic-facing, C-terminal half. D-glucose serves as both a metabolite and a hormone-like signal that regulates plant cell proliferation. High D-glucose arrests cell proliferation, but Arabidopsis mutants lacking AtRGS1 are insensitive to high concentrations of D-glucose. Conversely, plants ectopically expressing AtRGS1 are hypersensitive to sugars. D-glucose, but not L-glucose, causes rapid internalization of a AtRGS1:GFP fusion protein. These results raise the possibility that AtRGS1 is a glucose receptor that controls cell proliferation through regulation of the active state of its cognate G-protein complex.