Regulation of V‐ATPases by reversible disassembly

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Abstract
V‐ATPases consist of a complex of peripheral subunits containing catalytic sites for ATP hydrolysis, the V1 sector, attached to several membrane subunits containing a proton pore, the V0 sector. ATP‐driven proton transport requires structural and functional coupling of the two sectors, but in vivo, the interaction between the V1 and V0 sectors is dynamic and is regulated by extracellular conditions. Dynamic instability appears to be a general characteristic of V‐ATPases and, in yeast cells, the assembly state of V‐ATPases is governed by glucose availability. The structural and functional implications of reversible disassembly of V‐ATPases are discussed.