On the ligand binding profile and desensitization of plant ionotropic glutamate receptor (iGluR)-like channels functioning in MAMP-triggered Ca2+ influx

Abstract

The generation of intracellular microbe-associated molecular pattern (MAMP)-triggered Ca2+ transients was recently demonstrated to involve ionotropic Glutamate Receptor (iGluR)-like channels in Arabidopsis and tobacco. Here we elaborate on our previous findings and refine our insights in the putative agonist binding profile and potential mode of desensitization of MAMP-activated plant iGluRs. Based on results from pharmacological inhibition and desensitization experiments, we propose that plant iGluRs complexes responsible for the MAMP-triggered Ca2+ signature have a binding profile that combines the specificities of mammalian NMDA-and non-NMDA types of iGluRs, possibly reflecting the evolutionary history of plant and animal iGluR. We further hypothesize that, analogous to the mammalian NMDA-NR1 receptor, desensitization of plant iGluR-like channels might involve binding of the ubiquitous Ca2+ sensor calmodulin to a cytoplasmic C-terminal domain. © 2012 Landes Bioscience.