Proton translocation driven by ATP hydrolysis in V‐ATPases

@article{KawasakiNishi2003ProtonTD,
  title={Proton translocation driven by ATP hydrolysis in V‐ATPases},
  author={Shoko Kawasaki-Nishi and Tsuyoshi Nishi and Michael Forgac},
  journal={FEBS Letters},
  year={2003},
  volume={545}
}
Structure and Regulation of Plant Vacuolar H+-ATPase
The vacuolar proton translocating ATPase (V-ATPase) is an essential protein complex present in all eukaryotes which functions as ATP-driven rotary motor. In higher eukaryotes, the V-ATPase consists
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The C subunit has very important functions in terms of controlling the regulation of the reversible dissociation of V-ATPases.
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The hypothesis that PAM serves as a luminal pH‐sensor, regulating V‐ATPase action by altering its assembly status is supported, which supports the hypothesis that the biosynthetic and endocytic pathways of peptidergic cells are characterized by progressive luminal acidification.
The vacuolar proton-ATPase plays a major role in several membrane-bounded organelles in Paramecium
TLDR
The V-ATPase was found to be crucial for osmoregulation, the phagocytotic pathway and the biogenesis of dense core secretory granules in Paramecium.
Characterisation of the human H⁺-ATPase a4 subunit.
TLDR
Findings indicate a direct link between V-ATPase and glycolysis, via the C-terminus of the pump's a subunit, and suggest a novel regulatory mechanismBetween V- ATPase function and energy supply.
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References

SHOWING 1-10 OF 136 REFERENCES
Structural changes linked to proton translocation by subunit c of the ATP synthase
TLDR
Conformational changes between the protonated and deprotonated forms of subunit c provide the structural basis for an explicit mechanism to explain coupling of proton translocation by FO to the rotation of subunits within the core of F1.
The cellular biology of proton-motive force generation by V-ATPases.
TLDR
A novel gene family in which null mutations cause pleiotropic effects on metal-ion resistance or on the sensitivity and distribution of membrane proteins in different targets was discovered and is termed VTC (Vacuolar Transporter Chaperon) and four genes in S. cerevisiae that belong to the family.
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.
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
Regulation and Reversibility of Vacuolar H+-ATPase*
TLDR
Results indicate that V-ATPase is a reversible enzyme and vacuolar membranes may have a regulatory mechanism for maintaining a constant membrane potential.
Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation
TLDR
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.
Three-dimensional Structure of the Vacuolar ATPase Proton Channel by Electron Microscopy*
TLDR
The three-dimensional structure of the proton channel domain of the vacuolar ATPase from bovine brain clathrin-coated vesicles is determined by electron microscopy at 21 Å resolution.
Molecular architecture of the rotary motor in ATP synthase.
TLDR
An electron density map obtained from crystals of a subcomplex of yeast mitochondrial ATP synthase shows a ring of 10 c subunits whose extensive contact between the c ring and the stalk suggests that they may rotate as an ensemble during catalysis.
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.
Structural biology: Proton-powered turbine of a plant motor
TLDR
This work has imaged the ATP synthase from leaf chloroplasts by using atomic force microscopy and, surprisingly, finds that its turbine has 14 subunits, arranged in a cylindrical ring.
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