Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 104, Issue 44, Pages 17317-17322Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.0704751104
Keywords
D-glucose; G protein-coupled receptor; guanine nucleoticle cycle; RGS protein; GTPase-accelerating protein
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Funding
- NIGMS NIH HHS [R01 GM074268, R01GM074268, F32 GM076944, GM076944, R01GM065989, R01 GM065989] Funding Source: Medline
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Heterotrimeric G protein signaling is important for cell-proliferative and glucose-sensing signal transduction pathways in the model plant, organism Arabidopsis thaliana. AtRGS1 is a seven-transmembrane, RGS domain-containing protein that is a putative membrane receptor for D-glucose. Here we show, by using FRET, that D-glucose alters the interaction between the AtGPA1 and AtRGS1 in vivo. AtGPA1 is a unique heterotrimeric G protein a subunit that is constitutively GTP-bound given its high spontaneous nucleotide exchange coupled with slow GTP hydrolysis. Analysis of a point mutation in AtRGS1 that abrogates GTPase-accelerating activity demonstrates that the regulation of AtGPA1 GTP hydrolysis mediates sugar signal transduction during Arabidopsis development, in contrast to animals where nucleotide exchange is the limiting step in the heterotrimeric G protein nucleotide cycle.
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