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Many Proline Residues in the Extracellular Domain Contribute to Glycine Receptor Function.

Prolines in signaling proteins are of particular interest because they have a range of unique properties that may be critical for function. Here we show that many proline residues in the extracellular domain (ECD) of the glycine receptor are involved in the correct functioning of this ligand-gated ion channel. We explore their role by creating mutant receptors, expressing them in cells, and using fluorescent membrane potential sensitive dye to monitor receptor activity. We then interpret the changes in receptor parameters using structural information from the open and closed states of the receptor. The data reveal that substitution with alanine of ten of the 13 Pro residues in the ECD alters the function of the receptor: one substitution ablates function, six cause a decrease in the EC50, and three cause an increase. Only three of these mutants result in EC50 values similar to WT. The nonfunctional mutant, Pro30Ala, was further probed in oocytes, and the data suggest a role in both expression and function. Examination of the locations of sensitive Pro residues in the receptor and identification of potential interactions with nearby residues reveal how these residues could contribute to the correct functioning of this typical pentameric ligand-gated ion channel.