Biology:ATP6V1B2
 Generic protein structure example |
V-type proton ATPase subunit B, brain isoform is an enzyme that in humans is encoded by the ATP6V1B2 gene.[1][2][3]
This gene encodes a component of vacuolar ATPase (V-ATPase), a multisubunit enzyme that mediates acidification of eukaryotic intracellular organelles. V-ATPase dependent organelle acidification is necessary for such intracellular processes as protein sorting, zymogen activation, receptor-mediated endocytosis, and synaptic vesicle proton gradient generation. V-ATPase is composed of a cytosolic V1 domain and a transmembrane V0 domain. The V1 domain consists of three A, three B, and two G subunits, as well as a C, D, E, F, and H subunit. The V1 domain contains the ATP catalytic site. The protein encoded by this gene is one of two V1 domain B subunit isoforms and is the only B isoform highly expressed in osteoclasts.[3]
In melanocytic cells ATP6V1B2 gene expression may be regulated by MITF.[4]
References
- ↑ "An mRNA from human brain encodes an isoform of the B subunit of the vacuolar H(+)-ATPase". J Biol Chem 265 (29): 17428–31. Nov 1990. doi:10.1016/S0021-9258(18)38179-1. PMID 2145275.
- ↑ "Revised nomenclature for mammalian vacuolar-type H+ -ATPase subunit genes". Mol Cell 12 (4): 801–3. Oct 2003. doi:10.1016/S1097-2765(03)00397-6. PMID 14580332.
- ↑ 3.0 3.1 "Entrez Gene: ATP6V1B2 ATPase, H+ transporting, lysosomal 56/58kDa, V1 subunit B2". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=526.
- ↑ "Novel MITF targets identified using a two-step DNA microarray strategy". Pigment Cell Melanoma Res. 21 (6): 665–76. 2008. doi:10.1111/j.1755-148X.2008.00505.x. PMID 19067971.
External links
- Human ATP6V1B2 genome location and ATP6V1B2 gene details page in the UCSC Genome Browser.
Further reading
- "The vacuolar H+-ATPase: a universal proton pump of eukaryotes.". Biochem. J. 324 (3): 697–712. 1997. doi:10.1042/bj3240697. PMID 9210392.
- "Structure, function and regulation of the vacuolar (H+)-ATPase.". Annu. Rev. Cell Dev. Biol. 13: 779–808. 1998. doi:10.1146/annurev.cellbio.13.1.779. PMID 9442887.
- "Vacuolar and plasma membrane proton-adenosinetriphosphatases.". Physiol. Rev. 79 (2): 361–85. 1999. doi:10.1152/physrev.1999.79.2.361. PMID 10221984.
- Forgac M (1999). "Structure and properties of the vacuolar (H+)-ATPases.". J. Biol. Chem. 274 (19): 12951–4. doi:10.1074/jbc.274.19.12951. PMID 10224039.
- Kane PM (1999). "Introduction: V-ATPases 1992-1998.". J. Bioenerg. Biomembr. 31 (1): 3–5. doi:10.1023/A:1001884227654. PMID 10340843.
- "Animal plasma membrane energization by proton-motive V-ATPases.". BioEssays 21 (8): 637–48. 1999. doi:10.1002/(SICI)1521-1878(199908)21:8<637::AID-BIES3>3.0.CO;2-W. PMID 10440860.
- "The vacuolar (H+)-ATPases--nature's most versatile proton pumps.". Nat. Rev. Mol. Cell Biol. 3 (2): 94–103. 2002. doi:10.1038/nrm729. PMID 11836511.
- "Proton translocation driven by ATP hydrolysis in V-ATPases.". FEBS Lett. 545 (1): 76–85. 2003. doi:10.1016/S0014-5793(03)00396-X. PMID 12788495.
- Morel N (2004). "Neurotransmitter release: the dark side of the vacuolar-H+ATPase.". Biol. Cell 95 (7): 453–7. doi:10.1016/S0248-4900(03)00075-3. PMID 14597263.
- "Selectively amplified expression of an isoform of the vacuolar H(+)-ATPase 56-kilodalton subunit in renal intercalated cells.". Proc. Natl. Acad. Sci. U.S.A. 89 (8): 3541–5. 1992. doi:10.1073/pnas.89.8.3541. PMID 1373501. Bibcode: 1992PNAS...89.3541N.
- "Transcriptional regulation of the vacuolar H(+)-ATPase B2 subunit gene in differentiating THP-1 cells.". J. Biol. Chem. 270 (13): 7320–9. 1995. doi:10.1074/jbc.270.13.7320. PMID 7706273.
- "Heterogeneity of vacuolar H(+)-ATPase: differential expression of two human subunit B isoforms.". Biochem. J. 303 (1): 191–8. 1994. doi:10.1042/bj3030191. PMID 7945239.
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