Cysteine-mediated Cross-linking Indicates That Subunit C of the V-ATPase Is in Close Proximity to Subunits E and G of the V1 Domain and Subunit a of the V0 Domain*

@article{Inoue2005CysteinemediatedCI,
  title={Cysteine-mediated Cross-linking Indicates That Subunit C of the V-ATPase Is in Close Proximity to Subunits E and G of the V1 Domain and Subunit a of the V0 Domain*},
  author={Takao Inoue and Michael Forgac},
  journal={Journal of Biological Chemistry},
  year={2005},
  volume={280},
  pages={27896 - 27903}
}
The vacuolar (H+)-ATPases (V-ATPases) are multisubunit complexes responsible for ATP-dependent proton transport across both intracellular and plasma membranes. The V-ATPases are composed of a peripheral domain (V1) that hydrolyzes ATP and an integral domain (V0) that conducts protons. Dissociation of V1 and V0 is an important mechanism of controlling V-ATPase activity in vivo. The crystal structure of subunit C of the V-ATPase reveals two globular domains connected by a flexible linker (Drory… 

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Function and Subunit Interactions of the N-terminal Domain of Subunit a (Vph1p) of the Yeast V-ATPase*
TLDR
Results suggest that a localized region of the N-terminal domain is important in anchoring the peripheral stator in V1V0, suggesting that in vivo dissociation of the V-ATPase generates a V0 domain that does not passively conduct protons.
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TLDR
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The Tether Connecting Cytosolic (N Terminus) and Membrane (C Terminus) Domains of Yeast V-ATPase Subunit a (Vph1) Is Required for Assembly of V0 Subunit d*
TLDR
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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.
The N-terminal domain of the V-ATPase subunit 'a' is regulated by pH in vitro and in vivo
TLDR
The purification and biochemical characterization of the N-terminal domain of subunit 'a', Vph1N, which has been suggested to act as a pH sensor in mammalian cells are presented, and pH-dependent oligomerization of this domain in vivo and in vitro is demonstrated.
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