PANX1
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
Disruptions of this gene have been associated to melanoma tumor progression.[2]
References
- ↑ 1.0 1.1 "Entrez Gene: Pannexin 1". Retrieved 2012-04-11.
- ↑ Penuela S, Gyenis L, Ablack A, Churko JM, Berger AC, Litchfield DW, Lewis JD, Laird DW (June 2012). "Loss of pannexin 1 attenuates melanoma progression by reversion to a melanocytic phenotype". J Biol Chem 287 (34): 29184–93. doi:10.1074/jbc.M112.377176. PMID 22753409.
Further reading
- Pelegrin, P.; Surprenant, A. (2006). "Pannexin-1 mediates large pore formation and interleukin-1β release by the ATP-gated P2X7 receptor". The EMBO Journal 25 (21): 5071–5082. doi:10.1038/sj.emboj.7601378. PMC 1630421. PMID 17036048.
- Bruzzone, R.; Hormuzdi, S. G.; Barbe, M. T.; Herb, A.; Monyer, H. (2003). "Pannexins, a family of gap junction proteins expressed in brain". Proceedings of the National Academy of Sciences 100 (23): 13644–13649. doi:10.1073/pnas.2233464100. PMC 263867. PMID 14597722.
- Reyes, J. P.; Hernández-Carballo, C. Y.; Pérez-Flores, G.; Pérez-Cornejo, P.; Arreola, J. (2009). "Lack of coupling between membrane stretching and pannexin-1 hemichannels". Biochemical and Biophysical Research Communications 380 (1): 50–53. doi:10.1016/j.bbrc.2009.01.021. PMC 2670310. PMID 19150332.
- Orloff, M.; Peterson, C.; He, X.; Heald, S.; Yang, B.; Bebek, Y. -R.; Romigh, G.; Song, T.; Wu, J. H.; David, W.; Cheng, S.; Meltzer, Y.; Eng, S. J.; Eng, C. (2011). "Germline Mutations in MSR1, ASCC1, and CTHRC1 in Patients with Barrett Esophagus and Esophageal Adenocarcinoma". JAMA: the Journal of the American Medical Association 306 (4): 410–419. doi:10.1001/jama.2011.1029. PMC 3574553. PMID 21791690.
- Ambrosi, C.; Gassmann, O.; Pranskevich, J. N.; Boassa, D.; Smock, A.; Wang, J.; Dahl, G.; Steinem, C.; Sosinsky, G. E. (2010). "Pannexin1 and Pannexin2 Channels Show Quaternary Similarities to Connexons and Different Oligomerization Numbers from Each Other". Journal of Biological Chemistry 285 (32): 24420–24431. doi:10.1074/jbc.M110.115444. PMC 2915678. PMID 20516070.
- Woehrle, T.; Yip, L.; Elkhal, A.; Sumi, Y.; Chen, Y.; Yao, Y.; Insel, P. A.; Junger, W. G. (2010). "Pannexin-1 hemichannel-mediated ATP release together with P2X1 and P2X4 receptors regulate T-cell activation at the immune synapse". Blood 116 (18): 3475–3484. doi:10.1182/blood-2010-04-277707. PMC 2981474. PMID 20660288.
- Boassa, D.; Ambrosi, C.; Qiu, F.; Dahl, G.; Gaietta, G.; Sosinsky, G. (2007). "Pannexin1 Channels Contain a Glycosylation Site That Targets the Hexamer to the Plasma Membrane". Journal of Biological Chemistry 282 (43): 31733–31743. 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, T. L.; Usman, N.; Staroverov, D.; Lukyanov, S.; Panchin, Y. (2004). "The mammalian pannexin family is homologous to the invertebrate innexin gap junction proteins". Genomics 83 (4): 706–716. doi:10.1016/j.ygeno.2003.09.025. PMID 15028292.
- Bhalla-Gehi, R.; Penuela, S.; Churko, J. M.; Shao, Q.; Laird, D. W. (2010). "Pannexin1 and Pannexin3 Delivery, Cell Surface Dynamics, and Cytoskeletal Interactions". Journal of Biological Chemistry 285 (12): 9147–9160. doi:10.1074/jbc.M109.082008. PMC 2838334. PMID 20086016.