Close

GLRB Membrane Protein Introduction

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
Gene Name GLRB
Aliases Glycine receptor 58 kDa subunit
Organism Homo sapiens (Human)
UniProt ID P48167
Transmembrane Times 4
Length (aa) 497
Sequence MKFLLTTAFLILISLWVEEAYSKEKSSKKGKGKKKQYLCPSQQSAEDLARVPANSTSNILNRLLVSYDPRIRPNFKGIPVDVVVNIFINSFGSIQETTMDYRVNIFLRQKWNDPRLKLPSDFRGSDALTVDPTMYKCLWKPDLFFANEKSANFHDVTQENILLFIFRDGDVLVSMRLSITLSCPLDLTLFPMDTQRCKMQLESFGYTTDDLRFIWQSGDPVQLEKIALPQFDIKKEDIEYGNCTKYYKGTGYYTCVEVIFTLRRQVGFYMMGVYAPTLLIVVLSWLSFWINPDASAARVPLGIFSVLSLASECTTLAAELPKVSYVKALDVWLIACLLFGFASLVEYAVVQVMLNNPKRVEAEKARIAKAEQADGKGGNVAKKNTVNGTGTPVHISTLQVGETRCKKVCTSKSDLRSNDFSIVGSLPRDFELSNYDCYGKPIEVNNGLGKSQAKNNKKPPPAKPVIPTAAKRIDLYARALFPFCFLFFNVIYWSIYL

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.

Structure of the GLRB protein. Fig.1 Structure of the GLRB protein.

Application of GLRB Membrane Protein in Literature

  1. Wu Q.J., et al. GLRB variants regulate nearby gene expression in human brain tissues. Sci Rep. 2017, 7(1): 13326. PubMed ID: 29042589

    The study reveals that both rs17035816 and rs7688285 variants could significantly regulate the expression of PDGFC and GLRB gene.

  2. Lueken U., et al. Modulation of defensive reactivity by GLRB allelic variation: converging evidence from an intermediate phenotype approach. Transl Psychiatry. 2017, 7(9): e1227. PubMed ID: 28872638

    The findings provide translational evidence for glycine neurotransmission as a modulator of the brain's evolutionary old dynamic defensive system.

  3. Deckert J., et al. GLRB allelic variation associated with agoraphobic cognitions, increased startle response and fear network activation: a potential neurogenetic pathway to panic disorder. Mol Psychiatry. 2017, 22(10): 1431-1439. PubMed ID: 28167838

    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.

  4. Del Pino I., et al. Proteomic analysis of glycine receptor β subunit (GlyRβ)-interacting proteins: evidence for syndapin I regulating synaptic glycine receptors. J Biol Chem. 2014, 289(16): 11396-409. PubMed ID: 24509844

    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.

  5. James V.M., et al. Novel missense mutations in the glycine receptor β subunit gene (GLRB) in startle disease. Neurobiol Dis. 2013, 52:137-49. PubMed ID: 23238346

    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

To obtain the soluble and functional target protein, the versatile Magic™ membrane protein production platform in Creative Biolabs enables many flexible options, from which you can always find a better match for your particular project. Aided by our versatile Magic™ anti-membrane protein antibody discovery platform, we also provide customized anti-GLRB antibody development services.


As a leading service provider, Creative Biolabs is proud to present our professional service in membrane protein preparation and help you with the research of membrane proteins. Please do not hesitate to inquire us for more details.

Online Inquiry

Verification code
Click image to refresh the verification code.

CONTACT US

45-1 Ramsey Road, Shirley, NY 11967, USA
Call us at:
USA: 1-631-381-2994
Europe: 44-207-097-1828
Fax: 1-631-207-8356
Email:
Our customer service representatives are available 24 hours a day, 7 days a week. Contact Us