Journal of Bioenergetics and Biomembranes

, Volume 35, Issue 4, pp 313–321

Assembly and Regulation of the Yeast Vacuolar H+-ATPase


DOI: 10.1023/A:1025724814656

Cite this article as:
Kane, P.M. & Smardon, A.M. J Bioenerg Biomembr (2003) 35: 313. doi:10.1023/A:1025724814656


The yeast vacuolar proton-translocating ATPase (V-ATPase) is an excellent model for V-ATPases in all eukaryotic cells. Activity of the yeast V-ATPase is reversibly down-regulated by disassembly of the peripheral (V1) sector, which contains the ATP-binding sites, from the membrane (V0) sector, which contains the proton pore. A similar regulatory mechanism has been found in Manduca sexta and is believed to operate in other eukaryotes. We are interested in the mechanism of reversible disassembly and its implications for V-ATPase structure. In this review, we focus on (1) characterization of the yeast V-ATPase stalk subunits, which form the interface between V1 and V0, (2) potential mechanisms of silencing ATP hydrolytic activity in disassembled V1 sectors, and (3) the structure and function of RAVE, a recently discovered complex that regulates V-ATPase assembly.

V-ATPasevacuoleacidificationvma mutantproton pumpRAVEyeaststalk

Copyright information

© Plenum Publishing Corporation 2003

Authors and Affiliations

  1. 1.Department of Biochemistry and Molecular BiologySUNY Upstate Medical UniversitySyracuse