GLRA3 Membrane Protein Introduction

Introduction of GLRA3

The Glycine receptor subunit alpha-3 is a protein that in humans is encoded by the GLRA3 gene. The protein is a subunit of the glycine receptor (GlyR). Glycine receptors belong to the cys-loop family of ligand-gated ion channels and are responsible for mediating the inhibitory effects of glycine. They are widely distributed throughout the CNS, particularly within the hippocampus, spinal cord, and brain stem. The glycine receptor consists of two subunits, α and β, and functions as a pentamer. The protein encoded by this gene is an alpha subunit and can bind strychnine. Alternative splicing results in multiple transcript variants. Glycine receptors (GlyRs) are homomeric or heteromeric ligand-gated chloride channels formed respectively by α subunits (α1-α4) or by a combination of α and β subunits. GlyR subunits display regional and temporal specificities in their patterns of expression. The mRNA of GlyR α1 and GlyR α3 can only be detected postnatally, with strong expression in the spinal cord.

Function of GLRA3 Membrane Protein

Glycine receptors are ligand-gated chloride channels. The opening of the channel is triggered by extracellular glycine. The channel characteristics are depending on the subunit composition. Heteropentameric channels show faster channel closure. Glycine receptor subunit alpha-3 plays a key role in the down-regulation of neuronal excitability and contributes to the generation of inhibitory postsynaptic currents and increased pain perception in response to increased prostaglandin E2 levels. Glycine receptors (GlyR) mediate fast inhibitory transmission in the vertebrate CNS. The disruption of glycinergic transmission through inherited mutations can cause panic disease in humans. Many startle mutations in GlyRs provide useful clues to the function of the channel domains. The role of GlyRα3 in inflammatory pain has already reported, which provides new insights into the potentiation of structure-based design of GlyR modulators for the treatment of neuropathic pain. In addition, loss of α3-GlyRs compromises suprathreshold auditory nerve activity, but not outer hair cell function. Functional α3 glycine receptors are also present in various regions of the forebrain and play roles in the regulation of neuronal excitability in the forebrain.

Fig.1 Glycine receptor alpha-3, homopentamer + 5 glycine (l.blue-red) + 5 strychnine (green-red) + 1 NAG (purple-red) + 5 Zn (d.green), Human.

Application of GLRA3 Membrane Protein in Literature

1. Dlugaiczyk J., et al. Loss of glycine receptors containing the α3 subunit compromises auditory nerve activity, but not outer hair cell function. Hear Res. 2016, 337: 25-34 PubMed ID: 27208792
   
   

   The study reveals that loss of α3-GlyRs compromises suprathreshold auditory nerve activity, but not outer hair cell function.

2. McCracken L.M., et al. Glycine receptor α3 and α2 subunits mediate tonic and exogenous agonist-induced currents in forebrain. Proc Natl Acad Sci U S A. 2017, 114(34): E7179-E7186. PubMed ID: 28784756
   
   

   The article reports that glycine receptor α3 and α2 play roles in the regulation of neuronal excitability in the forebrain. Functional α2 and α3 glycine receptors are present in various regions of the forebrain.

3. Schaefermeier P., et al. Hippocampal Characteristics and Invariant Sequence Elements Distribution of GLRA2 and GLRA3 C-to-U Editing. Mol Syndromol. 2017, 8(2): 85-92. PubMed ID: 28611548
   
   

   The article reports the distribution of hippocampal features and invariant sequence elements edited by GLRA2 and GLRA3 C-to-U.

4. Kono Y., et al. Presynaptic facilitation of glycinergic mIPSC is reduced in mice lacking α3 glycine receptor subunits. Neuroscience. 2016, 320:1-7. PubMed ID: 26851771
   
   

   Authors in this group find that presynaptic glycine release in the hypoglossal nucleus is partially depending on GlyR α3. In Glra3 knockout mice, the baseline glycine synaptic transmission to the nucleus of the hypoglossal motor neurons is quite normal.

5. Huang X., et al. Crystal structures of human glycine receptor α3 bound to a novel class of analgesic potentiators. Nat Struct Mol Biol. 2017, 24(2): 108-113. PubMed ID: 27991902
   
   

   The article provides new insights into the potentiation of cysteine-loop receptors through positive allosteric modulators and is promising in structure-based design of GlyR modulators for the treatment of neuropathic pain.

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