A Glutamate Receptor-Like Gene AtGLR2.5 With Its Unusual Splice Variant Has a Role in Mediating Glutamate-Elicited...

The occurrence of external L-glutamate at the Arabidopsis root tip triggers major changes in root architecture, but the mechanism of -L-Glu sensing is unknown. Members of the family of GLUTAMATE RECEPTOR-LIKE (GLR) proteins are known to act as amino acid-gated Ca²⁺-permeable channels and to have signalling roles in diverse plant processes. To investigate the possible role of GLRs in the root architectural response to L-Glu, we screened a collection of mutants with T-DNA insertions in each of the 20 AtGLR genes. Reduced sensitivity of root growth to L-Glu was found in mutants of one gene, GLR2.5. Interestingly, GLR2.5 was found to apparently produce four transcript variants encoding hypothetical proteins of 169-720 amino acids. One of these transcripts, GLR2.5c, encodes a truncated GLR protein lacking both the conserved amino-terminal domain and part of the ligand-binding domain. When a glr2.5 mutant was transformed with a construct constitutively expressing GLR2.5c, both L-Glu sensitivity of root growth and L-Glu-elicited Ca²⁺ currents in root tip protoplasts were restored. These results, along with homology modelling of the truncated ligand-binding domain of GLR2.5c, suggest that GLR2.5c has a regulatory or scaffolding role in heteromeric GLR complex(es) that may involve triggering the root architectural response to L-Glu.