PANX1

Pannexin 1
Identifiers
Symbols	PANX1 ; MRS1; PX1; UNQ2529
External IDs	OMIM: 608420 HomoloGene: 49416 IUPHAR: 735 GeneCards: PANX1 Gene
Gene ontology Molecular function • protease binding • receptor binding • calcium channel activity • leak channel activity • ion channel binding • protein heterodimerization activity • actin filament binding • gap junction hemi-channel activity • scaffold protein binding Cellular component • endoplasmic reticulum • endoplasmic reticulum membrane • plasma membrane • gap junction • membrane • integral component of membrane • bleb • protein complex Biological process • response to ischemia • cation transport • calcium ion transport • cell-cell signaling • synaptic transmission • response to ATP • protein hexamerization • nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway • innate immune response • positive regulation of interleukin-1 alpha secretion • positive regulation of interleukin-1 beta secretion • calcium ion transmembrane transport Sources: Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	24145	55991
Ensembl	ENSG00000110218	ENSMUSG00000031934
UniProt	Q96RD7	Q9JIP4
RefSeq (mRNA)	NM_015368	NM_019482
RefSeq (protein)	NP_056183	NP_062355
Location (UCSC)	Chr 11: 94.13 – 94.18 Mb	Chr 9: 15.01 – 15.05 Mb
PubMed search

Pannexin 1 is a protein in humans that is encoded by the PANX1 gene.^[1]

The protein encoded by this gene belongs to the innexin family. Innexin family members are the structural components of gap junctions. This protein and pannexin 2 are abundantly expressed in central nerve system (CNS) and are coexpressed in various neuronal populations. Studies in Xenopus oocytes suggest that this protein alone and in combination with pannexin 2 may form cell type-specific gap junctions with distinct properties.^[1]

Clinical relevance

Truncating mutations in this gene have been shown to promote breast cancer metastasis to the lungs by allowing cancer cells to survive mechanical stretch in the microcirculation. ^[2]

Disruptions of this gene have been associated to melanoma tumor progression.^[3]

References

1. "Entrez Gene: Pannexin 1". Retrieved 2012-04-11.
2. Furlow PW, Zhang S, Soong TD, Halberg N, Goodarzi H, Mangrum C, Wu YG, Elemento O, Tavazoie SF (July 2015). "Mechanosensitive pannexin-1 channels mediate microvascular metastatic cell survival.". Nature Cell Biology (17): 943–952. doi:10.1038/ncb3194. PMID 26098574.
3. Penuela S, Gyenis L, Ablack A, Churko JM, Berger AC, Litchfield DW, Lewis JD, Laird DW (Aug 2012). "Loss of pannexin 1 attenuates melanoma progression by reversion to a melanocytic phenotype". The Journal of Biological Chemistry 287 (34): 29184–93. doi:10.1074/jbc.M112.377176. PMID 22753409.

Further reading

• Pelegrin P, Surprenant A (Nov 2006). "Pannexin-1 mediates large pore formation and interleukin-1beta release by the ATP-gated P2X7 receptor". The EMBO Journal 25 (21): 5071–82. doi:10.1038/sj.emboj.7601378. PMC 1630421. PMID 17036048.
• Bruzzone R, Hormuzdi SG, Barbe MT, Herb A, Monyer H (Nov 2003). "Pannexins, a family of gap junction proteins expressed in brain". Proceedings of the National Academy of Sciences of the United States of America 100 (23): 13644–9. doi:10.1073/pnas.2233464100. PMC 263867. PMID 14597722.
• Reyes JP, Hernández-Carballo CY, Pérez-Flores G, Pérez-Cornejo P, Arreola J (Feb 2009). "Lack of coupling between membrane stretching and pannexin-1 hemichannels". Biochemical and Biophysical Research Communications 380 (1): 50–3. doi:10.1016/j.bbrc.2009.01.021. PMC 2670310. PMID 19150332.
• Orloff M, Peterson C, He X, Ganapathi S, Heald B, Yang YR, Bebek G, Romigh T, Song JH, Wu W, David S, Cheng Y, Meltzer SJ, Eng C (Jul 2011). "Germline mutations in MSR1, ASCC1, and CTHRC1 in patients with Barrett esophagus and esophageal adenocarcinoma". JAMA 306 (4): 410–9. doi:10.1001/jama.2011.1029. PMC 3574553. PMID 21791690.
• Ambrosi C, Gassmann O, Pranskevich JN, Boassa D, Smock A, Wang J, Dahl G, Steinem C, Sosinsky GE (Aug 2010). "Pannexin1 and Pannexin2 channels show quaternary similarities to connexons and different oligomerization numbers from each other". The Journal of Biological Chemistry 285 (32): 24420–31. doi:10.1074/jbc.M110.115444. PMC 2915678. PMID 20516070.
• Woehrle T, Yip L, Elkhal A, Sumi Y, Chen Y, Yao Y, Insel PA, Junger WG (Nov 2010). "Pannexin-1 hemichannel-mediated ATP release together with P2X1 and P2X4 receptors regulate T-cell activation at the immune synapse". Blood 116 (18): 3475–84. doi:10.1182/blood-2010-04-277707. PMC 2981474. PMID 20660288.
• Boassa D, Ambrosi C, Qiu F, Dahl G, Gaietta G, Sosinsky G (Oct 2007). "Pannexin1 channels contain a glycosylation site that targets the hexamer to the plasma membrane". The Journal of Biological Chemistry 282 (43): 31733–43. doi:10.1074/jbc.M702422200. PMID 17715132.
• Baranova A, Ivanov D, Petrash N, Pestova A, Skoblov M, Kelmanson I, Shagin D, Nazarenko S, Geraymovych E, Litvin O, Tiunova A, Born TL, Usman N, Staroverov D, Lukyanov S, Panchin Y (Apr 2004). "The mammalian pannexin family is homologous to the invertebrate innexin gap junction proteins". Genomics 83 (4): 706–16. doi:10.1016/j.ygeno.2003.09.025. PMID 15028292.
• Bhalla-Gehi R, Penuela S, Churko JM, Shao Q, Laird DW (Mar 2010). "Pannexin1 and pannexin3 delivery, cell surface dynamics, and cytoskeletal interactions". The Journal of Biological Chemistry 285 (12): 9147–60. doi:10.1074/jbc.M109.082008. PMC 2838334. PMID 20086016.