The Where, When, and How of Organelle Acidification by the Yeast Vacuolar H+-ATPase

  title={The Where, When, and How of Organelle Acidification by the Yeast Vacuolar H+-ATPase},
  author={Patricia M. Kane},
  journal={Microbiology and Molecular Biology Reviews},
  pages={177 - 191}
  • P. Kane
  • Published 1 March 2006
  • Biology
  • Microbiology and Molecular Biology Reviews
SUMMARY All eukaryotic cells contain multiple acidic organelles, and V-ATPases are central players in organelle acidification. Not only is the structure of V-ATPases highly conserved among eukaryotes, but there are also many regulatory mechanisms that are similar between fungi and higher eukaryotes. These mechanisms allow cells both to regulate the pHs of different compartments and to respond to changing extracellular conditions. The Saccharomyces cerevisiae V-ATPase has emerged as an important… 

Figures from this paper

Structural comparison of the vacuolar and Golgi V-ATPases from Saccharomyces cerevisiae
It is shown that purified V-ATPase complexes containing Vph1p have higher ATPase activity than complexes containing Stv1p and that the relative difference in activity depends on the presence of lipids.
Vacuolar H+-ATPase—an enzyme for all seasons
It is known that V-ATPase is vital for many more physiological and biochemical processes than anticipated when the enzyme was discovered a few decades ago.
Structure and Roles of V-type ATPases.
Regulation of Vacuolar Proton-translocating ATPase Activity and Assembly by Extracellular pH*
This work proposes that when alternative mechanisms of vacuolar acidification are not available, maintaining V-ATPase activity becomes a priority, and the pump is not down-regulated in response to energy limitation, and suggests that integrated pH and metabolic inputs determine the final assembly state and activity of the V- ATPase.
The vacuolar (H+)-ATPase: subunit arrangement and in vivo regulation
Cysteine-mediated cross-linking has been used to localize subunit isoforms within the V-ATPase complex and to investigate the helical interactions between subunits within the integral V0 domain.
Structure and regulation of the vacuolar ATPases.
New insights into the regulation of V-ATPase-dependent proton secretion.
The vacuolar H(+)-ATPase (V-ATPase) is a key player in several aspects of cellular function, including acidification of intracellular organelles and regulation of extracellular pH. In specialized
Vacuolar-type proton ATPase as regulator of membrane dynamics in multicellular organisms
The non-classical, beyond proton-pumping function of the vacuolar-type ATPase in exo/endocytic systems is focused and overviewed.
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.


Assembly and Regulation of the Yeast Vacuolar H+-ATPase
This review focuses on characterization of the yeast V-ATPase stalk subunits, which form the interface between V1 and V0, potential mechanisms of silencing ATP hydrolytic activity in disassembled V1 sectors, and the structure and function of RAVE, a recently discovered complex that regulates V- ATPase assembly.
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.
Vacuolar and plasma membrane proton-adenosinetriphosphatases.
V-ATPases function exclusively as ATP-dependent proton pumps and are the main if not the only primary energy source for numerous transport systems in these organelles in eukaryotic cells.
Vacuolar H(+)-ATPase.
Cellular role of the V-ATPase in Neurospora crassa: analysis of mutants resistant to concanamycin or lacking the catalytic subunit A.
To understand further the mechanism of inhibition by these antibiotics and the physiological role of the enzyme in the cell, isolated mutants of the filamentous fungus Neurospora crassa that are resistant to concanamycin are isolated.
Alternative Mechanisms of Vacuolar Acidification in H+-ATPase-deficient Yeast*
Although NH3 can act as a cell-permeant proton scavenger, NH4 + may function as a protonophore, facilitating equilibration of the pH across the plasma and vacuolar membranes of yeast.
Molecular Characterization of the Yeast Vacuolar H+-ATPase Proton Pore*
Structural differences within the membrane-spanning domains of both V0 and F0 may account for the unique properties of the ATP-hydrolyzing V-ATPase compared with the ATP -generating F-type ATP synthase.
Structure and regulation of insect plasma membrane H(+)V-ATPase.
Recent advances in understanding the structure of the V(1) and V(o) complexes and of the regulation of the enzyme's biosynthesis and ion-transport activity will be discussed.