P2RX7

Purinergic receptor P2X, ligand-gated ion channel, 7
Identifiers
Symbols	P2RX7; MGC20089; P2X7
External IDs	OMIM: 602566 MGI: 1339957 HomoloGene: 1925 GeneCards: P2RX7 Gene
Gene Ontology Molecular function • lipopolysaccharide binding • purinergic nucleotide receptor activity • receptor activity • extracellular ATP-gated cation channel activity • receptor binding • ion channel activity • protein binding • ATP binding • protein homodimerization activity Cellular component • cytoplasm • plasma membrane • integral to plasma membrane • membrane • bleb Biological process • regulation of sodium ion transport • ion transport • cell surface receptor linked signaling pathway • positive regulation of calcium ion transport into cytosol • sensory perception of pain • positive regulation of bone mineralization • bleb assembly • response to ATP • purinergic nucleotide receptor signaling pathway • regulation of apoptosis • negative regulation of MAPKKK cascade • negative regulation of bone resorption • positive regulation of cytolysis • pore complex assembly • positive regulation of interleukin-1 beta secretion • positive regulation of cytoskeleton organization • regulation of killing of cells of other organism • membrane depolarization Sources: Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	5027	18439
Ensembl	ENSG00000089041	ENSMUSG00000029468
UniProt	Q99572	Q3UN00
RefSeq (mRNA)	NM_002562.5	NM_001038839
RefSeq (protein)	NP_002553.3	NP_001033928
Location (UCSC)	Chr 12: 121.57 – 121.62 Mb	Chr 5: 123.09 – 123.14 Mb
PubMed search	[1]	[2]

P2X purinoceptor 7 is a protein that in humans is encoded by the P2RX7 gene.^[1][2]

The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel and is responsible for ATP-dependent lysis of macrophages through the formation of membrane pores permeable to large molecules. Multiple alternatively spliced variants which would encode different isoforms have been identified although some fit nonsense-mediated decay (NMD) criteria.^[3]

In melanocytic cells P2RX7 gene expression may be regulated by MITF^[4].

Recruitment of pannexin

Activation of the P2RX7 receptor by ATP leads to recruitment of pannexin pores^[5] which allow small molecules such as ATP to leak out of cells. This allows further activation of purinergic receptors and physiological responses such a spreading cytoplasmic waves of calcium^[6]

See also

• Purinergic receptor
• P2X receptor

References

1. ^ Rassendren F, Buell GN, Virginio C, Collo G, North RA, Surprenant A (Apr 1997). "The permeabilizing ATP receptor, P2X7. Cloning and expression of a human cDNA". J Biol Chem 272 (9): 5482–6. doi:10.1074/jbc.272.9.5482. PMID 9038151. 
2. ^ Buell GN, Talabot F, Gos A, Lorenz J, Lai E, Morris MA, Antonarakis SE (Feb 1999). "Gene structure and chromosomal localization of the human P2X7 receptor". Receptors Channels 5 (6): 347–54. PMID 9826911. 
3. ^ "Entrez Gene: P2RX7 purinergic receptor P2X, ligand-gated ion channel, 7". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5027. 
4. ^ Hoek KS, Schlegel NC, Eichhoff OM et al. (2008). "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971. 
5. ^ Iglesias, R.; Locovei, S.; Roque, A.; Alberto, A. P.; Dahl, G.; Spray, D. C.; Scemes, E. (2008). "P2X7 receptor-Pannexin1 complex: Pharmacology and signaling". AJP: Cell Physiology 295 (3): C752–C760. doi:10.1152/ajpcell.00228.2008. PMC 2544446. PMID 18596211. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2544446.  edit
6. ^ Boison, D.; Chen, J. -F.; Fredholm, B. B. (2009). "Adenosine signaling and function in glial cells". Cell Death and Differentiation 17 (7): 1071–1082. doi:10.1038/cdd.2009.131. PMC 2885470. PMID 19763139. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2885470.  edit

Further reading

• Gartland A, Buckley KA, Hipskind RA, Bowler WB, Gallagher JA. (2003). "P2 receptors in bone--modulation of osteoclast formation and activity via P2X7 activation". Crit Rev Eukaryot Gene Expr. 13 (2–4): 237–42. doi:10.1615/CritRevEukaryotGeneExpr.v13.i24.150. PMID 14696970. 
• Gartland A, Buckley KA, Bowler WB, Gallagher JA. (2003). "Blockade of the pore-forming P2X7 receptor inhibits formation of multinucleated human osteoclasts in vitro". Calcif Tissue Int. 72 (4): 361–9. doi:10.1007/s00223-002-2098-y. PMID 12874700. 
• Bowler WB, Buckley KA, Gartland A, Hipskind RA, Bilbe G, Gallagher JA. (2001). "Extracellular nucleotide signaling: a mechanism for integrating local and systemic responses in the activation of bone remodeling". Bone 28 (5): 507–12. doi:10.1016/S8756-3282(01)00430-6. PMID 11344050. 
• Gartland A, Hipskind RA, Gallagher JA, Bowler WB. (2001). "Expression of a P2X7 receptor by a subpopulation of human osteoblasts". J Bone Miner Res . 16 (5): 846–56. doi:10.1359/jbmr.2001.16.5.846. PMID 11341329. 
• Gartland A, Buckley KA, Hipskind RA, Perry MJ, Tobias JH, Buell G, Chessell I, Bowler WB, Gallagher JA. (2003). "Multinucleated osteoclast formation in vivo and in vitro by P2X7 receptor-deficient mice". Crit Rev Eukaryot Gene Expr. 13 (2–4): 243–53. doi:10.1615/CritRevEukaryotGeneExpr.v13.i24.160. PMID 14696971. 
• North RA (2002). "Molecular physiology of P2X receptors". Physiol. Rev. 82 (4): 1013–67. doi:10.1152/physrev.00015.2002. PMID 12270951. 
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298. 
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149. 
• Gu BJ, Zhang W, Worthington RA et al. (2001). "A Glu-496 to Ala polymorphism leads to loss of function of the human P2X7 receptor". J. Biol. Chem. 276 (14): 11135–42. doi:10.1074/jbc.M010353200. PMID 11150303. 
• Kim M, Jiang LH, Wilson HL et al. (2002). "Proteomic and functional evidence for a P2X7 receptor signalling complex". EMBO J. 20 (22): 6347–58. doi:10.1093/emboj/20.22.6347. PMC 125721. PMID 11707406. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125721. 
• Worthington RA, Smart ML, Gu BJ et al. (2002). "Point mutations confer loss of ATP-induced human P2X(7) receptor function". FEBS Lett. 512 (1–3): 43–6. doi:10.1016/S0014-5793(01)03311-7. PMID 11852049. 
• Wiley JS, Dao-Ung LP, Gu BJ et al. (2002). "A loss-of-function polymorphic mutation in the cytolytic P2X7 receptor gene and chronic lymphocytic leukaemia: a molecular study". Lancet 359 (9312): 1114–9. doi:10.1016/S0140-6736(02)08156-4. PMID 11943260. 
• Wilson HL, Wilson SA, Surprenant A, North RA (2002). "Epithelial membrane proteins induce membrane blebbing and interact with the P2X7 receptor C terminus". J. Biol. Chem. 277 (37): 34017–23. doi:10.1074/jbc.M205120200. PMID 12107182. 
• Atkinson L, Milligan CJ, Buckley NJ, Deuchars J (2002). "An ATP-gated ion channel at the cell nucleus". Nature 420 (6911): 42. doi:10.1038/420042a. PMID 12422208. 
• Budagian V, Bulanova E, Brovko L et al. (2003). "Signaling through P2X7 receptor in human T cells involves p56lck, MAP kinases, and transcription factors AP-1 and NF-kappa B". J. Biol. Chem. 278 (3): 1549–60. doi:10.1074/jbc.M206383200. PMID 12424250. 
• Sluyter R, Wiley JS (2003). "Extracellular adenosine 5'-triphosphate induces a loss of CD23 from human dendritic cells via activation of P2X7 receptors". Int. Immunol. 14 (12): 1415–21. doi:10.1093/intimm/dxf111. PMID 12456589. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241. 
• Wiley JS, Dao-Ung LP, Li C et al. (2003). "An Ile-568 to Asn polymorphism prevents normal trafficking and function of the human P2X7 receptor". J. Biol. Chem. 278 (19): 17108–13. doi:10.1074/jbc.M212759200. PMID 12586825. 
• Barden JA, Sluyter R, Gu BJ, Wiley JS (2003). "Specific detection of non-functional human P2X(7) receptors in HEK293 cells and B-lymphocytes". FEBS Lett. 538 (1–3): 159–62. doi:10.1016/S0014-5793(03)00172-8. PMID 12633871. 
• Verhoef PA, Estacion M, Schilling W, Dubyak GR (2003). "P2X7 receptor-dependent blebbing and the activation of Rho-effector kinases, caspases, and IL-1 beta release". J. Immunol. 170 (11): 5728–38. PMID 12759456. 
• Greig AV, Linge C, Terenghi G et al. (2003). "Purinergic receptors are part of a functional signaling system for proliferation and differentiation of human epidermal keratinocytes". J. Invest. Dermatol. 120 (6): 1007–15. doi:10.1046/j.1523-1747.2003.12261.x. PMID 12787128. 
• Denlinger LC, Sommer JA, Parker K et al. (2003). "Mutation of a dibasic amino acid motif within the C terminus of the P2X7 nucleotide receptor results in trafficking defects and impaired function". J. Immunol. 171 (3): 1304–11. PMID 12874219. 

External links

• MeSH P2RX7+protein,+human

Ionotropic glutamates

Ligand-gated only	AMPA (1, 2, 3, 4) · Kainate (1, 2, 3, 4, 5)
Voltage- and ligand-gated	NMDA (1, 2A, 2B, 2C, 2D, 3A, 3B, L1A, L1B)
‘Orphan’	GluD (δ1, δ2)

ATP-gated channels

Purinergic receptors

P2X (1, 2, 3, 4, 5, 6, 7)

B trdu: iter (nrpl/grfl/cytl/horl), csrc (lgic, enzr, gprc, igsr, intg, nrpr/grfr/cytr), itra (adap, gbpr, mapk), calc, lipd; path (hedp, wntp, tgfp+mapp, notp, jakp, fsap, hipp, tlrp)