Structural insights into long-distance signal transduction pathways mediated by plant glutamate receptor-like channels

In recent years, studies have shed light on the physiological role of plant glutamate receptor-like channels (GLRs). However, the mechanism by which these channels are activated, and in particular, what is the physiological role of their binding to amino acids, remains elusive. The first direct biochemical demonstration that the Arabidopsis thaliana GLR3.3 isoform binds glutamate and other amino acids in a low micromolar range of concentrations was reported only recently. The first crystal structures of the ligand-binding domains of AtGLR3.3 and AtGLR3.2 isoforms also have been released. We foresee that these new experimental pieces of evidence provide the basis for a better understanding of how GLRs are activated and modulated in different physiological responses.

Automated summary

Recent studies have highlighted the physiological role of plant glutamate receptor-like channels (GLRs), but the mechanisms of activation and the physiological significance of amino acid binding are still unclear. Recent biochemical and structural evidence regarding Arabidopsis thaliana GLR3.3 isoform binding to glutamate and other amino acids provides a foundation for better understanding the activation and modulation of GLRs in various physiological responses.