Introduction of GLRB
Glycine receptor subunit beta (GLRB) is a protein that in humans is encoded by the GLRB gene. Glycine receptor subunit beta belongs to the glycine receptor family. The inhibitory glycine receptor mediates postsynaptic inhibition in the spinal cord and other regions of the central nervous system. Inhibitory glycine receptors (GlyRs) are ligand-gated chloride channels enriched in the spinal cord, brainstem, and retina, consisting of heteropentameric combinations of ligand-binding GlyR α subunits (α1-α4) together with the GlyR β subunit. Each GlyR subunit is composed of an N-terminal extracellular domain and four α-helical membrane-spanning domains (M1-M4). M3 and M4 are linked by a long intracellular domain containing binding sites for a variety of intracellular factors. Both GlyR α and β subunits play an active role in agonist binding. But until recently, the GlyR β subunit was widely considered to play a structural role in heteromeric GlyRs. In part, this was due to the pivotal role of the GlyR β subunit in mediating high-affinity interactions with the synaptic clustering molecule gephyrin, which in turn controls the dynamic localization of GlyRs at synaptic sites.
|Basic Information of GLRB|
|Protein Name||Glycine receptor subunit beta|
|Aliases||Glycine receptor 58 kDa subunit|
|Organism||Homo sapiens (Human)|
Function of GLRB Membrane Protein
The beta subunit of the glycine receptor functions as a neurotransmitter-gated ion channel, playing a major role in inhibitory neurotransmission. It produces hyperpolarization by increased chloride conductance due to binding of glycine to the receptor. Mutations of the GLRB gene cause startle disease (also known as congenital stiff-person syndrome or hereditary hyperekplexia), a disease characterized by muscular rigidity. Alternative splicing results in multiple transcript variants. Recently, a genome-wide association of GLRB with categorical (panic disorder (PD)) and dimensional (agoraphobia (AG)) forms of fear and anxiety has been reported, in particular for rs7688285 which was associated with GLRB expression changes in postmortem tissue and reporter gene assays. Defects in the adult GlyR isoform (α1β) also have an important role in these diseases. Mutations in GLRA1, encoding the GlyR α1 subunit, are the major genetic cause of startle disease/hyperekplexia in humans.
Fig.1 Structure of the GLRB protein.
Application of GLRB Membrane Protein in Literature
The study reveals that both rs17035816 and rs7688285 variants could significantly regulate the expression of PDGFC and GLRB gene.
The findings provide translational evidence for glycine neurotransmission as a modulator of the brain's evolutionary old dynamic defensive system.
The article reports that GLRB allelic variation is associated with agoraphobic cognitions, increased startle response and fear network activation, providing evidence that non-coding, although functional GLRB gene polymorphisms may predispose to panic disorder.
Authors in this group find evidence for syndapin I regulating synaptic glycine receptors in the proteomic analysis of glycine receptor β subunit (GlyRβ)-interacting proteins.
The article reveals the existence of novel missense mutations in the glycine receptor β subunit gene (GLRB) in startle disease, providing a potential genetic explanation for "slight" forms of over-agonism.
GLRB Preparation Options
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