Assembly and regulation of the yeast vacuolar H+-ATPase.
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.
Kane
Patricia M
PM
Department of Biochemistry and Molecular Biology, SUNY Upstate Medical University, 750 East Adams Street, Syracuse, New York 13210, USA. kanepm@upstate.edu
Smardon
Anne M
AM
D005656:Fungal Proteins / Q000378:metabolism / Q000502:physiology; D020409:Molecular Motor Proteins; D011499:Protein Processing, Post-Translational; D021122:Protein Subunits; D025262:Vacuolar Proton-Translocating ATPases / Q000096:biosynthesis* / Q000378:metabolism*; D015003:Yeasts / Q000201:enzymology
D005656:Fungal Proteins; D020409:Molecular Motor Proteins; D021122:Protein Subunits; D025262:Vacuolar Proton-Translocating ATPases