GLR3.2 belongs to clade III of the plant glutamate receptor-like (GLR) family, which shares structural homology with animal ionotropic glutamate receptors (iGluRs) but exhibits distinct ligand-binding properties . Key features include:
Structure: Contains a bilobed ligand-binding domain (LBD) that adopts a clamshell conformation, activated by amino acids like glycine and asparagine .
Localization: Primarily localized to the phloem of Arabidopsis roots, particularly near sieve plates .
Function: Forms heteromeric channels with GLR3.4 to regulate calcium influx, influencing lateral root primordia development and positioning .
The GLR3.2 antibody has been instrumental in:
Protein Localization Studies: Immunohistochemistry and GFP-tagged constructs revealed phloem-specific expression in roots .
Interaction Analysis: Co-immunoprecipitation and biophotonic assays demonstrated physical interaction between GLR3.2 and GLR3.4 .
Mutant Phenotyping: Characterized glr3.2 knockout mutants, which exhibit hyperproduction of lateral root primordia due to disrupted calcium signaling .
The table below summarizes studies utilizing GLR3.2-targeted approaches:
GLR3.2 research highlights its role in:
Root Development: Restricting lateral root primordia overproduction via phloem-localized signaling .
Stress Responses: Potential involvement in abiotic stress adaptation through Ca²⁺-mediated signaling .
Evolutionary Conservation: Structural parallels with iGluRs underscore conserved gating mechanisms across kingdoms .