Electrophysiological Signature of Homomeric and Heteromeric Glycine Receptor Channels.

ABSTRACT: Glycine receptors are chloride-permeable, ligand-gated ion channels and contribute to the inhibition of neuronal firing in the central nervous system or to facilitation of neurotransmitter release if expressed at presynaptic sites. Recent structure-function studies have provided detailed insights into the mechanisms of channel gating, desensitization, and ion permeation. However, most of the work has focused only on comparing a few isoforms, and among studies, different cellular expression systems were used. Here, we performed a series of experiments using recombinantly expressed homomeric and heteromeric glycine receptor channels, including their splice variants, in the same cellular expression system to investigate and compare their electrophysiological properties. Our data show that the

SUBMITTER: Raltschev C 

PROVIDER: S-EPMC5016189 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature