Regulation of V-ATPases by reversible disassembly

FEBS Lett. 2000 Mar 10;469(2-3):137-41. doi: 10.1016/s0014-5793(00)01265-5.


V-ATPases consist of a complex of peripheral subunits containing catalytic sites for ATP hydrolysis, the V(1) sector, attached to several membrane subunits containing a proton pore, the V(0) sector. ATP-driven proton transport requires structural and functional coupling of the two sectors, but in vivo, the interaction between the V(1) and V(0) 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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Adenosine Triphosphate / metabolism
  • Animals
  • Glucose / metabolism
  • Manduca / enzymology
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Protein Structure, Quaternary
  • Proton Pumps / chemistry
  • Proton Pumps / metabolism*
  • Proton-Translocating ATPases / chemistry
  • Proton-Translocating ATPases / metabolism*
  • Saccharomyces cerevisiae / chemistry
  • Saccharomyces cerevisiae / enzymology
  • Vacuolar Proton-Translocating ATPases*


  • Membrane Proteins
  • Proton Pumps
  • Adenosine Triphosphate
  • Vacuolar Proton-Translocating ATPases
  • Proton-Translocating ATPases
  • Glucose