A Journey From Mammals to Yeast With Vacuolar H+-ATPase (V-ATPase)

Nathan Nelson*

*Corresponding author for this work

Research output: Contribution to journalShort surveypeer-review

67 Scopus citations


The vacuolar H+-ATPase (V-ATPase) is one of the most fundamental enzymes in nature. It functions in almost every eukaryotic cell and energizes a wide variety of organelles and membranes. V-ATPase has a structure and mechanism of action similar to F-ATPase and several of their subunits probably evolved from common ancestors. In eukaryotic cells, F-ATPase is confined to the semiautonomous organelles, chloroplasts and mitochondria, which contain their own genes that encode some of the F-ATPase subunits. In contrast to F-ATPases, whose primary function in eukaryotic cells is to form ATP at the expense of the protonmotive force (pmf), V-ATPases function exclusively as ATP-dependent proton pumps. The pmf generated by V-ATPases in organelles and membranes of eukaryotic cells is utilized as a driving force for numerous secondary transport processes. It was the survival of the yeast mutant without the active enzyme and yeast genetics that allowed the identification of genuine subunits of the V-ATPase. It also revealed special properties of individual subunits, factors that are involved in the enzyme's biogenesis and assembly, as well as the involvement of V-ATPase in the secretory pathway, endocytosis, and respiration. It may be the insect V-ATPase that unconventionally resides in the plasma membrane of their midgut, that will give the first structure resolution of this complex.

Original languageEnglish
Pages (from-to)281-289
Number of pages9
JournalJournal of Bioenergetics and Biomembranes
Issue number4
StatePublished - Aug 2003


FundersFunder number
Division of Loan Repayment
Bundesministerium für Bildung und Forschung


    • Assembly
    • Biogenesis
    • F-ATPase
    • Membrane energization
    • Protonmotive force
    • Slip
    • V-ATPase


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