Overview
- Peptide HISTLQVGETRC, corresponding to amino acid residues 394-405 of rat GlyRβ (Accession P20781). 2nd intracellular loop.
- Rat and mouse brain lysates (1:200-1:1000).
Western blot analysis of mouse (lanes 1 and 3) and rat (lanes 2 and 4) brain lysates:1,2. Anti-Glycine Receptor β Antibody (#AGR-014), (1:200).
3,4. Anti-Glycine Receptor β Antibody, preincubated with Glycine Receptor β Blocking Peptide (#BLP-GR014).
Glycine receptor β in mouse cerebellumFree-floating frozen brain sections from a paraformaldehyde-perfused mouse were incubated with rabbit anti-glycine receptor β antibody (#AGR-014. 1:300), followed by goat anti-rabbit secondary antibody conjugated to Alexa Fluor® 488 (green). A. Glycine receptor β immunoreactivity was observed in the Purkinje layer (P) and in single interneurons in the granule layer (arrow, GL). B. Pre-incubation of the primary antibody with the Glycine Receptor β Blocking Peptide (#BLP-GR014) suppressed the staining. Nuclear staining with DAPI (blue).
Glycine receptor β in rat substantia nigra pars compacta (SNC)Free-floating frozen brain sections from a paraformaldehyde-perfused rat were incubated with rabbit anti-glycine receptor β antibody (#AGR-014. 1:300), followed by goat anti-rabbit secondary antibody conjugated to Alexa Fluor® 488 (green). A. Glycine receptor β immunoreactivity was observed in the SNC (arrows). B. Pre-incubation of the primary antibody with the Glycine Receptor β Blocking Peptide (#BLP-GR014) suppressed the staining. Nuclear staining with DAPI (blue).
The amino acid glycine mediates neuronal inhibition by activating glycine receptors (GlyRs), which are ligand-gated chloride channels of the nicotinic acetylcholine receptor superfamily. GlyRs are known to mediate postsynaptic inhibition in spinal cord, brain stem and some higher brain regions1. GlyRs are members of the pentameric Cys-loop family of ionotropic neurotransmitter receptors.
GlyRs are composed of homologous α (α1-α4) and β subunits. Upon synthesis at the endoplasmic reticulum (ER), all GlyRα subunits can assemble into functional homopentamers that are inserted into the plasma membrane. In contrast, the GlyRβ subunit requires stoichiometric coassembly with GlyRα subunits for ER exit and cell surface expression. Each subunit consists of an extended N-terminal extracellular domain, four transmembrane domains, and a large intracellular loop between transmembrane domains 3 and 4. The β subunit is responsible for synaptic localization of the GlyRs by interacting with the postsynaptic scaffolding protein gephyrin. GlyRβ subunit is reported to interact with the proteins Vacuolar Protein Sorting 35 (Vps35) and Neurobeachin (Nbea)2.
GlyRβ mRNA is abundantly found throughout the late embryonic and postnatal brain3.
Mutations in GLRB, the gene encoding GlyRβ, have been discovered in patients with hyperekplexia4, in the mouse mutant spastic5 and the zebrafish bandoneon mutant6.
