Arabidopsis thaliana REGULATOR OF G PROTEIN SIGNALING 1 (AtRGS1, hereafter, RGS1) within the heterotrimeric G protein complex plays a role in sensing extracellular signals. High millimolar concentrations of some sugars induce RGS1 endocytosis and therefore G protein activation. However, this is not likely a direct, rather an indirect effect through a sugar metabolite. One metabolite at the plasma membrane where RGS1 resides is UDP-glucose (UDPG) produced by SUCROSE SYNTHASE (SUS) enzymes, previously shown to interact with RGS1. Our direct measurements indicate that the Kd for UDPG binding to RGS1 (2.4 µM) is consistent with UDPG activation of RGS1 with an EC50 of 17 µM to rapidly trigger G protein activation ... More
Arabidopsis thaliana REGULATOR OF G PROTEIN SIGNALING 1 (AtRGS1, hereafter, RGS1) within the heterotrimeric G protein complex plays a role in sensing extracellular signals. High millimolar concentrations of some sugars induce RGS1 endocytosis and therefore G protein activation. However, this is not likely a direct, rather an indirect effect through a sugar metabolite. One metabolite at the plasma membrane where RGS1 resides is UDP-glucose (UDPG) produced by SUCROSE SYNTHASE (SUS) enzymes, previously shown to interact with RGS1. Our direct measurements indicate that the Kd for UDPG binding to RGS1 (2.4 µM) is consistent with UDPG activation of RGS1 with an EC50 of 17 µM to rapidly trigger G protein activation within minutes. RGS1 associates directly with SUS1 and SUS4, exhibiting affinities (Kd = 161 nM and 106 nM, respectively) that are markedly tighter than the corresponding Km values for UDPG formation (40 µM and 70 µM, respectively). Therefore, SUS may be one source for this RGS1 ligand in a manner analogous to “metabolite funneling” in enzymology. UDPG induces rapid phosphorylation of RGS1 at the C-terminal phosphorylation cluster, a site previously implicated in RGS1 endocytosis and G protein activation. UDPG activation of RGS1 changes the global transcript profiles in various processes, largely involving plant defense. These results provide the first molecular evidence for UDPG as a newly recognized low-molecular weight signal controlling key aspects of plant physiology.
