V-type proton ATPase 116 kDa subunit a isoform 2 also known as V-ATPase 116 kDa isoform a2 is an enzyme that in humans is encoded by the ATP6V0A2gene.[1][2][3]
V-ATPase 116 kDa isoform a2 is a subunit of the vacuolarATPase (v-ATPase), an heteromultimeric enzyme that is present in intracellular vesicles and in the plasma membrane of specialized cells, and which is essential for the acidification of diverse cellular components. V-ATPase consists of a membrane peripheral V(1) domain for ATP hydrolysis, and an integral membrane V(0) domain for proton translocation. The subunit encoded by this gene is a component of the V(0) domain.[3]
Clinical significance
Mutations in this gene are a cause of both cutis laxa type II and wrinkly skin syndrome.[3]
References
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↑Kornak U, Reynders E, Dimopoulou A, van Reeuwijk J, Fischer B, Rajab A, Budde B, Nurnberg P, Foulquier F, Lefeber D, Urban Z, Gruenewald S, Annaert W, Brunner HG, van Bokhoven H, Wevers R, Morava E, Matthijs G, Van Maldergem L, Mundlos S (Dec 2007). "Impaired glycosylation and cutis laxa caused by mutations in the vesicular H+-ATPase subunit ATP6V0A2". Nat Genet. 40 (1): 32–34. doi:10.1038/ng.2007.45. PMID18157129.
Nishi T, Forgac M (2002). "The vacuolar (H+)-ATPases--nature's most versatile proton pumps". Nat. Rev. Mol. Cell Biol. 3 (2): 94–103. doi:10.1038/nrm729. PMID11836511.
Kawasaki-Nishi S, Nishi T, Forgac M (2003). "Proton translocation driven by ATP hydrolysis in V-ATPases". FEBS Lett. 545 (1): 76–85. doi:10.1016/S0014-5793(03)00396-X. PMID12788495.
Smith AN, Lovering RC, Futai M, et al. (2003). "Revised nomenclature for mammalian vacuolar-type H+ -ATPase subunit genes". Mol. Cell. 12 (4): 801–803. doi:10.1016/S1097-2765(03)00397-6. PMID14580332.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet. 36 (1): 40–45. doi:10.1038/ng1285. PMID14702039.
Derks R, Beaman K (2005). "Regeneration and tolerance factor modulates the effect of adenosine triphosphate-induced interleukin 1 beta secretion in human macrophages". Hum. Immunol. 65 (7): 676–682. doi:10.1016/j.humimm.2004.04.006. PMID15301855.
Lattuada D, Mangioni S, Viganò P, et al. (2005). "The placental immunomodulatory cytokine regeneration and tolerance factor is also expressed by both human cycling and early pregnant endometrium". Am. J. Reprod. Immunol. 52 (3): 224–231. doi:10.1111/j.1600-0897.2004.00210.x. PMID15373763.
Hurtado-Lorenzo A, Skinner M, El Annan J, et al. (2006). "V-ATPase interacts with ARNO and Arf6 in early endosomes and regulates the protein degradative pathway". Nat. Cell Biol. 8 (2): 124–136. doi:10.1038/ncb1348. PMID16415858.
Olsen JV, Blagoev B, Gnad F, et al. (2006). "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks". Cell. 127 (3): 635–648. doi:10.1016/j.cell.2006.09.026. PMID17081983.
Ntrivalas E, Gilman-Sachs A, Kwak-Kim J, Beaman K (2007). "The N-terminus domain of the a2 isoform of vacuolar ATPase can regulate interleukin-1beta production from mononuclear cells in co-culture with JEG-3 choriocarcinoma cells". Am. J. Reprod. Immunol. 57 (3): 201–209. doi:10.1111/j.1600-0897.2006.00463.x. PMID17295899.
