Structural organization of the V-ATPase and its implications for regulatory assembly and disassembly.

@article{Diepholz2008StructuralOO,
  title={Structural organization of the V-ATPase and its implications for regulatory assembly and disassembly.},
  author={Meikel Diepholz and Michael B{\"o}rsch and Bettina B{\"o}ttcher},
  journal={Biochemical Society transactions},
  year={2008},
  volume={36 Pt 5},
  pages={
          1027-31
        }
}
V-ATPases (vacuolar ATPases) are membrane-bound multiprotein complexes that are localized in the endomembrane systems of eukaryotic cells and in the plasma membranes of some specialized cells. They couple ATP hydrolysis with the transport of protons across membranes. On nutrient shortage, V-ATPases disassemble into a membrane-embedded part (V0), which contains the proton translocation machinery, and an extrinsic part (V1), which carries the nucleotide-binding sites. Disassembly decouples ATP… 

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