ArticlePlant signaling & behavior2012
On the ligand binding profile and desensitization of plant ionotropic glutamate receptor (iGluR)-like channels functioning in MAMP-triggered Ca²⁺ influx.
Article in Plant signaling & behavior, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed, 8 citations in OpenAlex.
- The association of the serum free triiodothyronine to free thyroxine ratio with contrast-induced nephropathy and long-term outcomes in elective percutaneous coronary intervention: a retrospective study.BMC cardiovascular disorders · 2026Article
- Glutamate receptor-like channel3.3 is involved in mediating glutathione-triggered cytosolic calcium transients, transcriptional changes, and innate immunity responses in Arabidopsis.Plant physiology · 2013Article
- Ion channels in plants: from bioelectricity, via signaling, to behavioral actions.Plant signaling & behavior · 2013Article
- Inter-subunit interactions between glutamate-like receptors in Arabidopsis.Plant signaling & behavior · 2013Article
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Authors and funding
4 authors at 3 institutions in 3 countries.
Funding
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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 iGluR 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 iGluRs. 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.
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