Glutamate receptors are proteins that are essential for communication between brain cells (neurons), and function in brain processes including learning and memory. Mammalian glutamate receptors have evolved into a multi-gene family containing subtypes with genetic, functional and pharmacological similarities. Glutamate receptors are activated when they bind extracellular glutamate (ligand). The binding to the receptor allows the protein to open a channel (pore) through which ions flow across the neuron's membrane; converting a chemical signal (glutamate) into an electrical signal (membrane depolarization). The proposed study will test the hypothesis that one region common to all glutamate receptors (the M3-M4 extracellular domain) participates in a common mechanism to relay the signal between the ligand binding site and the pore (allosteric signal transduction). Elucidation of a conserved functional role of the M3-M4 extracellular domain would provide important insights into how ligand-gated ion channels function.
