Calcium entry mediated by GLR3.3, an Arabidopsis glutamate receptor with a broad agonist profile.

Article Details

Citation

Copy to clipboard

Qi Z, Stephens NR, Spalding EP

Calcium entry mediated by GLR3.3, an Arabidopsis glutamate receptor with a broad agonist profile.

Plant Physiol. 2006 Nov;142(3):963-71. Epub 2006 Sep 29.

PubMed ID

17012403 [ View in PubMed

]

Abstract

The amino acids glutamate (Glu) and glycine (Gly) trigger large, rapid rises in cytosolic Ca(2+) concentration and a concomitant rise in membrane potential (depolarization) in plants. The possibility that plant homologs of neuronal ionotropic glutamate receptors mediate these neuron-like ionic responses was tested in Arabidopsis (Arabidopsis thaliana) seedlings using a combination of Ca(2+) measurements, electrophysiology, and reverse genetics. The membrane depolarization triggered by Glu was greatly reduced or completely blocked in some conditions by mutations in GLR3.3, one of the 20 GLR genes in Arabidopsis. The same mutations completely blocked the associated rise in cytosolic Ca(2+). These results genetically demonstrate the participation of a glutamate receptor in the rapid ionic responses to an amino acid. The GLR3.3-independent component of the depolarization required Glu concentrations above 25 mum, did not display desensitization, and was strongly suppressed by increasing extracellular pH. It is suggested to result from H(+)-amino acid symport. Six amino acids commonly present in soils (Glu, Gly, alanine, serine, asparagine, and cysteine) as well as the tripeptide glutathione (gamma-glutamyl-cysteinyl-Gly) were found to be strong agonists of the GLR3.3-mediated responses. All other amino acids induced a small depolarization similar to the non-GLR, putative symporter component and in most cases evoked little or no Ca(2+) rise. From these results it may be concluded that sensing of six amino acids in the rhizosphere and perhaps extracellular peptides is coupled to Ca(2+) signaling through a GLR-dependent mechanism homologous to a fundamental component of neuronal signaling.

DrugBank Data that Cites this Article

Drug Targets

Drug	Target	Kind	Organism	Pharmacological Action	Actions
Glycine	Glycine receptor subunit alpha-2	Protein	Humans	Unknown	Ligand	Details