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 hydrolysis and proton translocation. Furthermore, the disassembled parts are inactive, leading to an efficient shutdown of ATP consumption. On restoring the nutrient levels, V1 and V0 reassemble and restore ATP-hydrolysis activity coupled with proton translocation. This reversible assembly/disassembly process has certain conformational constraints, which are best fulfilled by adopting a unique conformation before disassembly.
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October 2008
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Conference Article|
September 19 2008
Structural organization of the V-ATPase and its implications for regulatory assembly and disassembly
Meikel Diepholz;
*Structural and Computational Biology Unit, EMBL (European Molecular Biology Laboratory), Meyerhofstrasse 1, 69117 Heidelberg, Germany
1To whom correspondence should be addressed (email [email protected]).
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Michael Börsch;
Michael Börsch
†3. Physikalisches Institut, Universität Stuttgart, Pfaffenwaldring 57, 70550 Stuttgart, Germany
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Bettina Böttcher
Bettina Böttcher
1
*Structural and Computational Biology Unit, EMBL (European Molecular Biology Laboratory), Meyerhofstrasse 1, 69117 Heidelberg, Germany
1To whom correspondence should be addressed (email [email protected]).
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Publisher: Portland Press Ltd
Received:
March 28 2008
Online ISSN: 1470-8752
Print ISSN: 0300-5127
© The Authors Journal compilation © 2008 Biochemical Society
2008
Biochem Soc Trans (2008) 36 (5): 1027–1031.
Article history
Received:
March 28 2008
Citation
Meikel Diepholz, Michael Börsch, Bettina Böttcher; Structural organization of the V-ATPase and its implications for regulatory assembly and disassembly. Biochem Soc Trans 1 October 2008; 36 (5): 1027–1031. doi: https://doi.org/10.1042/BST0361027
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