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P2RX2 - Wikipedia, the free encyclopedia

P2RX2

From Wikipedia, the free encyclopedia


Purinergic receptor P2X, ligand-gated ion channel, 2
Identifiers
Symbol(s) P2RX2; MGC129601; P2X2
External IDs OMIM: 600844 MGI2665170 HomoloGene14251
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 22953 231602
Ensembl ENSG00000187848 ENSMUSG00000029503
Uniprot Q9UBL9 n/a
Refseq XM_001126081 (mRNA)
XP_001126081 (protein)
NM_153400 (mRNA)
NP_700449 (protein)
Location Chr 12: 131.71 - 131.71 Mb Chr 5: 110.58 - 110.58 Mb
Pubmed search [1] [2]

Purinergic receptor P2X, ligand-gated ion channel, 2, also known as P2RX2, is a human gene.[1]

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.[1]

Contents

[edit] See also

[edit] References

[edit] 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. 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. 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. 
  • Lynch KJ, Touma E, Niforatos W, et al. (1999). "Molecular and functional characterization of human P2X(2) receptors.". Mol. Pharmacol. 56 (6): 1171–81. PMID 10570044. 
  • 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. 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. 
  • Brake AJ, Wagenbach MJ, Julius D (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. 

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


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