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Significance Proton-pumping V-ATPases maintain the pH of intracellular compartments in all eukaryotic cells and the extracellular environment of specialized cells. V-ATPase dysfunction is associated with diseases including osteopetrosis, renal tubular acidosis, and cancer. Many subunits of mammalian V-ATPases exist as multiple isoforms that are expressed in an organelle-, cell-, or tissue-dependent manner, but the consequences of this diversity are not understood. In the yeastSaccharomyces cerevisiae , there are only two V-ATPase isoforms, making it an ideal system to study isoform-specific characteristics. Identifying similarities and differences in structure and function between V-ATPase isoforms improves our understanding of the enzyme’s diverse cellular functions.

Structural comparison of the vacuolar and Golgi V-ATPases from Saccharomyces cerevisiae