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

@article{Stevens1997StructureFA,
  title={Structure, function and regulation of the vacuolar (H+)-ATPase.},
  author={Tom H. Stevens and Michael Forgac},
  journal={Annual review of cell and developmental biology},
  year={1997},
  volume={13},
  pages={
          779-808
        }
}
The vacuolar (H+)-ATPases (or V-ATPases) function in the acidification of intracellular compartments in eukaryotic cells. The V-ATPases are multisubunit complexes composed of two functional domains. The peripheral V1 domain, a 500-kDa complex responsible for ATP hydrolysis, contains at least eight different subunits of molecular weight 70-13 (subunits A-H). The integral V0 domain, a 250-kDa complex, functions in proton translocation and contains at least five different subunits of molecular… 
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Structure, function and regulation of the vacuolar (H+)‐ATPases
Structural bases of physiological functions and roles of the vacuolar H(+)-ATPase.
An update in the structure, function, and regulation of V-ATPases: the role of the C subunit.
TLDR
The C subunit has very important functions in terms of controlling the regulation of the reversible dissociation of V-ATPases.
An update in the structure, function, and regulation of V-ATPases: the role of the C subunit
TLDR
The C subunit has very important functions in terms of controlling the regulation of the reversible dissociation of V-ATPases.
Assembly and Regulation of the Yeast Vacuolar H+-ATPase
TLDR
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.
Structure, function and regulation of the plant vacuolar H(+)-translocating ATPase.
Structure, mechanism and regulation of the clathrin-coated vesicle and yeast vacuolar H(+)-ATPases.
  • M. Forgac
  • Biology, Chemistry
    The Journal of experimental biology
  • 2000
TLDR
It is proposed that disulfide bond formation between conserved cysteine residues at the catalytic site of the V- ATPase plays an important role in regulating V-ATPase activity in vivo.
Composition and assembly of the yeast vacuolar H(+)-ATPase complex.
TLDR
The proton-translocating ATPase (H(+)-ATPase) found on the membrane of the yeast vacuole is the best characterized member of the V-type ATPase family and 14 genes, the majority designated VMA (for vacuolar membrane ATPase) encoding subunits of the enzyme complex are identified.
Building the Stator of the Yeast Vacuolar-ATPase
TLDR
This work has expressed subunits E and G in Escherichia coli as maltose binding protein fusion proteins and detected a specific interaction between these two subunits and proposed that the V-ATPase EG complex forms one of the peripheral stators similar to the one formed by the two copies of subunit b in F- ATPase.
Molecular Characterization of the Yeast Vacuolar H+-ATPase Proton Pore*
TLDR
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.
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References

SHOWING 1-10 OF 189 REFERENCES
Vacuolar H+-translocating ATPases from plants: Structure, function, and isoforms
TLDR
Isoforms of plant vacuolar ATPases are suggested by the variations in subunit composition observed among and within plant species, and by the presence of a small multigene family encoding the 16-k Da and 70-kDa subunits.
Subunit composition, biosynthesis, and assembly of the yeast vacuolar proton-translocating ATPase
TLDR
Initial results suggest that the peripheral and integral membrane subunits may be independently assembled in the vacuolar H+-ATPase complex and may be part of the final enzyme complex.
Structural conservation and functional diversity of V-ATPases
  • N. Nelson
  • Biology
    Journal of bioenergetics and biomembranes
  • 1992
TLDR
Genes encoding subunits of V-ATPase in yeast cells were interrupted to yield mutants that are devoid of the enzyme and are sensitive to pH and calcium concentrations in the medium, which shed light on the functional assembly of the enzymes in the vacuolar system.
Assembly and targeting of peripheral and integral membrane subunits of the yeast vacuolar H(+)-ATPase.
Subunit Composition and Organization of the Vacuolar H-ATPase from Oat Roots.
TLDR
Variations in subunit composition observed among several ATPases support the idea that distinct types of vacuolar H(+)-ATPases exist in plants.
Subunit G of the Vacuolar Proton Pump
TLDR
Reconstitution of ATP hydrolysis was achieved by combination of recombinant subunits A, B, C, and E with either recombinant G1 or G2, demonstrating the role of these isoforms in pump function.
A novel subunit of vacuolar H(+)-ATPase related to the b subunit of F-ATPases.
TLDR
A protein (M16) is identified that co-purifies with the V-ATPase complex from bovine chromaffin granules and exhibits a significant homology to subunit b of F- ATPases.
Comparison of the Coated‐Vesicle and Synaptic‐Vesicle Vacuolar (H+)‐ATPases
TLDR
This work is investigating several mechanisms of regulation of vacuolar acidification, including disulfide bond formation between cysteine residues located at the catalytic site, control of assembly of the peripheral and integral domains, and differential targeting of V-ATPases to different intracellular destinations using their interaction with organelle-specific adaptin complexes.
Site-directed Mutagenesis of the 100-kDa Subunit (Vph1p) of the Yeast Vacuolar (H+)-ATPase*
TLDR
The results suggest that the 100-kDa sub unit may be required for activity as well as assembly of the V-ATPase complex and that several charged residues in the last four putative transmembrane helices of this subunit may play a role in proton transport.
Chapter 5 Structure and function of the yeast vacuolar membrane H+-ATPase
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