Structure, function and regulation of the plant vacuolar H(+)-translocating ATPase

Biochim Biophys Acta. 2000 May 1;1465(1-2):17-36. doi: 10.1016/s0005-2736(00)00129-2.


The plant V-ATPase is a primary-active proton pump present at various components of the endomembrane system. It is assembled by different protein subunits which are located in two major domains, the membrane-integral V(o)-domain and the membrane peripheral V(1)-domain. At the plant vacuole the V-ATPase is responsible for energization of transport of ions and metabolites, and thus the V-ATPase is important as a 'house-keeping' and as a stress response enzyme. It has been shown that transcript and protein amount of the V-ATPase are regulated depending on metabolic conditions indicating that the expression of V-ATPase subunit is highly regulated. Moreover, there is increasing evidence that modulation of the holoenzyme structure might influence V-ATPase activity.

Publication types

  • Comparative Study
  • Review

MeSH terms

  • Enzyme Activation
  • Gene Expression Regulation, Enzymologic
  • Gene Expression Regulation, Plant
  • Membrane Proteins / chemistry
  • Membrane Proteins / metabolism*
  • Plant Proteins / chemistry
  • Plant Proteins / metabolism*
  • Proton-Translocating ATPases / chemistry
  • Proton-Translocating ATPases / genetics
  • Proton-Translocating ATPases / metabolism*


  • Membrane Proteins
  • Plant Proteins
  • Proton-Translocating ATPases