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

Meikel Diepholz, Michael Boersch, Bettina Boettcher

Research output: Contribution to journalArticlepeer-review

Abstract / Description of output

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 (V-0), which contains the proton translocation machinery, and an extrinsic part (V-1), 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, V-1 and V-0 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.

Original languageEnglish
Pages (from-to)1027-1031
Number of pages5
JournalBiochemical Society Transactions
Volume36
DOIs
Publication statusPublished - Oct 2008

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