P2RX2 Membrane Protein Introduction

Introduction of P2RX2

P2X purinoceptor 2 (P2RX2) is encoded by human P2RX1 gene, which is mapped to chromosome 12q24.33. Belonging to the family of purinoceptors for ATP, P2RX2 assembles as a trimer to form a ligand-gated ion channel gated by extracellular ATP. P2RX2 is widely expressed in several tissues, with the highest expression in hair cell stereocilia facing the endolymph, in Deiters cells within the perilymphatic compartment, and in afferent neurons of the spiral ganglion. In addition, P2RX2 is also detected in postsynaptic junctions at both inner and outer hair cells.

Function of P2RX2 Membrane Protein

As a member of ATP-gated P2X receptor cation channel family, P2RX2 enables the selective permeation of cation and its activity is regulated by the binding of extracellular adenosine 5'-triphosphate. It is documented that ATP-gated channels of sensory neurons are formed by a specific heteropolymerization of P2X receptor subunits and P2RX2 is an important component. P2RX2 is found to influence outer hair cells (OHCs) electromotility, a stimulus-induced change in hair cell length that functions as an amplifier to determine hearing sensitivity and frequency selectivity. In addition, P2RX2 is involved in many cellular responses, such as neuromuscular junctions (NMJ) formation, excitatory postsynaptic responses in sensory neurons, peristalsis, the perception of taste and hearing, the regulation of sound transduction and auditory neurotransmission. It can also regulate synaptic transmission between neurons and from neurons to smooth muscle, blood coagulation, skeletal muscle fiber development, urinary bladder smooth muscle contraction, etc.

Fig.1 A simulated trimeric model of P2RX2 in the repository of SWISS-MODEL. (Bienert, 2017)

Application of P2RX2 Membrane Protein in Literature

1. Chen M., et al. Identify Down syndrome transcriptome associations using integrative analysis of microarray database and correlation-interaction network. Hum Genomics. 2018, 12(1): 2. PubMed ID: 29351810
   
   

   This article finds that the most significant pathways related to the top Down syndrome critical region 9 co-expressed genes are shown to be associated with neuro-active ligand-receptor interaction (P2RX2, HTR4, GLP1R, UCN3, and UTS2R), calcium signaling pathway (P2RX2, CACNG4, HTR4, CACNA1F, and SLC8A3) by the KEGG, and GO analysis.

2. Bouzid A., et al. Down-expression of P2RX2, KCNQ5, ERBB3 and SOCS3 through DNA hypermethylation in elderly women with presbycusis. Biomarkers. 2018, 23(4): 347-356. PubMed ID: 29325454
   
   

   This article identifies P2RX2, KCNQ5, ERBB3, and SOCS3 to be involved in the progression of age-related hearing impairment through functional annotation and qRT-PCR.

3. Mittal R., et al. Characterization of ATPase Activity of P2RX2 Cation Channel. Front Physiol. 2016, 7: 186. PubMed ID: 27252659
   
   

   This article demonstrates that P2RX2 has the ATPase activity in cochlear neuroepithelium and in vitro studies. It finds that the P2RX2 V60L mutation, which can lead to human deafness, loses its ability to bind ATP, while the G353R mutation has no effect on ATP hydrolysis or binding .

4. Moteki H., et al. Hearing loss caused by a P2RX2 mutation identified in a MELAS family with a coexisting mitochondrial 3243AG mutation. Ann Otol Rhinol Laryngol. 2015, 124 Suppl 1: 177S-83S. PubMed ID: 25788561
   
   

   This report suggests that the loss of hearing caused by the mutation of P2RX2 may be influenced by the decrease in ATP production due to mitochondrial myopathy, encephalopathy, lactic acidosis, and stroke-like episodes(MELAS).

5. Faletra F., et al. A novel P2RX2 mutation in an Italian family affected by autosomal dominant nonsyndromic hearing loss. Gene. 2014, 534(2): 236-9. PubMed ID: 24211385
   
   

   This article reveals that the mutation of P2RX2 may have a possible role in causing autosomal dominant hereditary hearing loss.

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Reference

1. Bienert S, et al. (2017). The SWISS-MODEL Repository - new features and functionality. Nucleic Acids Res. 45: D313-D319.

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