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Vacuolar ATPases: rotary proton pumps in physiology and pathophysiology
  • M. Forgac
  • Biology
    Nature Reviews Molecular Cell Biology
  • 1 November 2007
The acidity of intracellular compartments and the extracellular environment is crucial to various cellular processes, including membrane trafficking, protein degradation, bone resorption and sperm maturation, and the V-ATPases represent attractive and potentially highly specific drug targets.
The vacuolar (H+)-ATPases — nature's most versatile proton pumps
The pH of intracellular compartments in eukaryotic cells is a carefully controlled parameter that affects many cellular processes, including intracellular membrane transport, prohormone processing
Structure, function and regulation of the vacuolar (H+)-ATPase.
Several mechanisms have been implicated in the regulation of vacuolar acidification in vivo, including control of pump density, regulation of assembly of V1 and V0 domains, disulfide bond formation, activator or inhibitor proteins, and regulation of counterion conductance.
Regulation and isoform function of the V-ATPases.
A number of mechanisms are employed to regulate V-ATPase activity in vivo, including reversible dissociation of the V(1) and V(0) domains, control of the tightness of coupling of proton transport and ATP hydrolysis, and selective targeting of V- ATPases to distinct cellular membranes.
Structure and function of vacuolar class of ATP-driven proton pumps.
  • M. Forgac
  • Chemistry, Medicine
    Physiological reviews
  • 1 July 1989
Function of a Subunit Isoforms of the V-ATPase in pH Homeostasis and in Vitro Invasion of MDA-MB231 Human Breast Cancer Cells*
The results suggest that the a4 isoform may be responsible for targeting V- ATPases to the plasma membrane of MB231 cells and that cell surface V-ATPases play a significant role in invasion.
Function, structure and regulation of the vacuolar (H+)-ATPases.
The Amino-terminal Domain of the Vacuolar Proton-translocating ATPase a Subunit Controls Targeting and in Vivo Dissociation, and the Carboxyl-terminal Domain Affects Coupling of Proton Transport and
The results suggest that whereas targeting and in vivo dissociation are controlled by sequences located in the amino-terminal domains of the subunit a isoforms, coupling efficiency is controlled by the carboxyl-Terminal region.
Yeast V-ATPase Complexes Containing Different Isoforms of the 100-kDa a-subunit Differ in Coupling Efficiency and in VivoDissociation*
The results suggest that dissociation of the V-ATPase complex in vivo is controlled both by the cellular environment and by the 100-kDa a-subunit isoform present in the complex.
Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation
It is suggested that Arg-735 is absolutely required for proton transport by the V-ATPases and is discussed in the context of a revised model of the topology of the 100-kDa subunit a.