P2RX2

Purinergic receptor P2X, ligand-gated ion channel, 2
Identifiers
SymbolsP2RX2 ; DFNA41; P2X2
External IDsOMIM: 600844 MGI: 2665170 HomoloGene: 14251 IUPHAR: 479 ChEMBL: 2531 GeneCards: P2RX2 Gene
RNA expression pattern
More reference expression data
Orthologs
SpeciesHumanMouse
Entrez22953231602
EnsemblENSG00000187848ENSMUSG00000029503
UniProtQ9UBL9Q8K3P1
RefSeq (mRNA)NM_001282164NM_001164833
RefSeq (protein)NP_001269093NP_001158305
Location (UCSC)Chr 12:
133.2 – 133.2 Mb		Chr 5:
110.34 – 110.34 Mb
PubMed search

P2X purinoceptor 2 is a protein that in humans is encoded by the P2RX2 gene.[1][2][3]

The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel. Binding to ATP mediates synaptic transmission between neurons and from neurons to smooth muscle. Six transcript variants encoding six distinct isoforms have been identified for this gene.[3]

See also

References

  1. ↑ Lynch KJ, Touma E, Niforatos W, Kage KL, Burgard EC, van Biesen T, Kowaluk EA, Jarvis MF (Dec 1999). "Molecular and functional characterization of human P2X(2) receptors". Mol Pharmacol 56 (6): 1171–81. PMID 10570044.
  2. ↑ Brake AJ, Wagenbach MJ, Julius D (Oct 1994). "New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor". Nature 371 (6497): 519–23. doi:10.1038/371519a0. PMID 7523952.
  3. ↑ 3.0 3.1 "Entrez Gene: P2RX2 purinergic receptor P2X, ligand-gated ion channel, 2".

Further reading

  • North RA (2002). "Molecular physiology of P2X receptors". Physiol. Rev. 82 (4): 1013–67. doi:10.1152/physrev.00015.2002. PMID 12270951.
  • Barrera NP, Ormond SJ, Henderson RM et al. (2005). "Atomic force microscopy imaging demonstrates that P2X2 receptors are trimers but that P2X6 receptor subunits do not oligomerize". J. Biol. Chem. 280 (11): 10759–65. doi:10.1074/jbc.M412265200. PMID 15657042.
  • Mason HS, Bourke S, Kemp PJ (2005). "Selective modulation of ligand-gated P2X purinoceptor channels by acute hypoxia is mediated by reactive oxygen species". Mol. Pharmacol. 66 (6): 1525–35. doi:10.1124/mol.104.000851. PMID 15331767.
  • Aschrafi A, Sadtler S, Niculescu C et al. (2004). "Trimeric architecture of homomeric P2X2 and heteromeric P2X1+2 receptor subtypes". J. Mol. Biol. 342 (1): 333–43. doi:10.1016/j.jmb.2004.06.092. PMID 15313628.
  • Boué-Grabot E, Emerit MB, Toulmé E et al. (2004). "Cross-talk and co-trafficking between rho1/GABA receptors and ATP-gated channels". J. Biol. Chem. 279 (8): 6967–75. doi:10.1074/jbc.M307772200. PMID 14660627.
  • Strausberg RL, Feingold EA, Grouse LH et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Järlebark LE, Housley GD, Raybould NP et al. (2003). "ATP-gated ion channels assembled from P2X2 receptor subunits in the mouse cochlea". Neuroreport 13 (15): 1979–84. doi:10.1097/00001756-200210280-00030. PMID 12395104.
  • Khakh BS, Zhou X, Sydes J et al. (2000). "State-dependent cross-inhibition between transmitter-gated cation channels". Nature 406 (6794): 405–10. doi:10.1038/35019066. PMID 10935636.
  • Brändle U, Spielmanns P, Osteroth R et al. (1997). "Desensitization of the P2X(2) receptor controlled by alternative splicing". FEBS Lett. 404 (2–3): 294–8. doi:10.1016/S0014-5793(97)00128-2. PMID 9119082.
  • Lewis C, Neidhart S, Holy C et al. (1995). "Coexpression of P2X2 and P2X3 receptor subunits can account for ATP-gated currents in sensory neurons". Nature 377 (6548): 432–5. doi:10.1038/377432a0. PMID 7566120.

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.