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 aminoterminal 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.