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© Marie Prévost, Institut Pasteur
Image of a portion of a Xenopus oocyte expressing a channel receptor.
Publication : ACS chemical neuroscience

Large Intracellular Domain-Dependent Effects of Positive Allosteric Modulators on Glycine Receptors

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in ACS chemical neuroscience - 29 Mar 2019

Lara CO, Burgos CF, Silva-Grecchi T, Muñoz-Montesino C, Aguayo LG, Fuentealba J, Castro PA, Guzmán JL, Corringer PJ, Yévenes GE, Moraga-Cid G

Link to Pubmed [PMID] – 30893555

ACS Chem Neurosci 2019 May;10(5):2551-2559

Glycine receptors (GlyRs) are members of the pentameric ligand-gated ionic channel family (pLGICs) and mediate fast inhibitory neurotransmission in the brain stem and spinal cord. The function of GlyRs can be modulated by positive allosteric modulators (PAMs). So far, it is largely accepted that both the extracellular (ECD) and transmembrane (TMD) domains constitute the primary target for many of these PAMs. On the other hand, the contribution of the intracellular domain (ICD) to the PAM effects on GlyRs remains poorly understood. To gain insight about the role of the ICD in the pharmacology of GlyRs, we examined the contribution of each domain using a chimeric receptor. Two chimeras were generated, one consisting of the ECD of the prokaryotic homologue Gloeobacter violaceus ligand-gated ion channel (GLIC) fused to the TMD of the human αGlyR lacking the ICD (Lily) and a second with the ICD (Lily-ICD). The sensitivity to PAMs of both chimeric receptors was studied using electrophysiological techniques. The Lily receptor showed a significant decrease in the sensitivity to four recognized PAMs. Remarkably, the incorporation of the ICD into the Lily background was sufficient to restore the wild-type αGlyR sensitivity to these PAMs. Based on these data, we can suggest that the ICD is necessary to form a pLGIC having full sensitivity to positive allosteric modulators.

https://www.ncbi.nlm.nih.gov/pubmed/30893555