Assembly and Regulation of the Yeast Vacuolar H+-ATPase

@article{Kane2003AssemblyAR,
  title={Assembly and Regulation of the Yeast Vacuolar H+-ATPase},
  author={Patricia M. Kane and Anne M. Smardon},
  journal={Journal of Bioenergetics and Biomembranes},
  year={2003},
  volume={35},
  pages={313-321}
}
  • P. Kane, A. Smardon
  • Published 1 August 2003
  • Biology, Chemistry
  • Journal of Bioenergetics and Biomembranes
The yeast vacuolar proton-translocating ATPase (V-ATPase) is an excellent model for V-ATPases in all eukaryotic cells. Activity of the yeast V-ATPase is reversibly down-regulated by disassembly of the peripheral (V1) sector, which contains the ATP-binding sites, from the membrane (V0) sector, which contains the proton pore. A similar regulatory mechanism has been found in Manduca sexta and is believed to operate in other eukaryotes. We are interested in the mechanism of reversible disassembly… 
Structural Studies of Saccharomyces cerevisiae V1-ATPase in the Stationary Phase of Yeast Cell Culture
TLDR
It was shown that by introducing a 3xFLAG tag at the C terminus of different V1-ATPase subunits, highly purified V 1- ATPase complex could be isolated and differed in the peripheral stalk subunit composition.
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.
The Where, When, and How of Organelle Acidification by the Yeast Vacuolar H+-ATPase
  • P. Kane
  • Biology
    Microbiology and Molecular Biology Reviews
  • 2006
TLDR
Current knowledge of the structure, function, and regulation of the V- ATPase in S. cerevisiae is discussed and the relationship between biosynthesis and transport of V-ATPase and compartment-specific regulation of acidification is examined.
Close-Up and Genomic Views of the Yeast Vacuolar H+-ATPase
  • P. Kane
  • Biology
    Journal of bioenergetics and biomembranes
  • 2005
TLDR
In this review, recent biochemical and genomic studies of the yeast V-ATPase are described, with a focus on the role of V1 subunit H in coupling ATP hydrolysis and proton pumping and identification of the full set of yeast haploid deletion mutants that exhibit the pH and calcium-sensitive growth characteristic of loss of V- ATPase activity.
Glu-44 in the Amino-terminal α-Helix of Yeast Vacuolar ATPase E Subunit (Vma4p) Has a Role for VoV1 Assembly*
TLDR
Results suggest that Glu-44 is one of the key functional residues for subunit interaction in the V-ATPase stalk complex that allows both efficient rotation catalysis and assembly.
Structural features and nucleotide-binding capability of the C subunit are integral to the regulation of the eukaryotic V1Vo ATPases.
  • G. Grüber
  • Biology, Chemistry
    Biochemical Society transactions
  • 2005
TLDR
Impressive progress has been made in elucidating the structure of the C subunit and its arrangement inside the V-ATPase, and nucleotide occupancy by subunit C, followed by conformational changes of this subunit has shed light on the mechanism of V-ATOR regulation.
Subunit Interactions at the V1-Vo Interface in Yeast Vacuolar ATPase*
TLDR
It is speculated that the spatial closeness of the aNT, Cfoot, and EG binding sites in the intact V-ATPase results in a high-avidity interaction that is able to resist the torque of rotational catalysis, and that reversible enzyme dissociation is initiated by breaking either the a NT(104–372)-Cfoot or aNT(104-372)-EG interaction by an as-yet unknown signaling mechanism.
Advances in targeting the vacuolar proton-translocating ATPase (V-ATPase) for anti-fungal therapy
TLDR
An overview of recent studies in mammals and hypothetical ways to target V-ATPase as an anti-fungal drug target as well as novel high-throughput methods for use in future drug discovery screens are discussed.
The C-H Peripheral Stalk Base: A Novel Component in V1-ATPase Assembly
TLDR
The formation of a CE3G3H sub-assembly appears to be unique to the dissociated V-ATPase and highlights the stator architecture in addition to revealing a possible intermediate in the assembly mechanism of the free V1-ATpase.
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
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 100 REFERENCES
Structure, function and regulation of the vacuolar (H+)-ATPase.
TLDR
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.
STRUCTURE, FUNCTION AND REGULATION OF THE VACUOLAR
TLDR
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.
Reversible Association between the V1and V0 Domains of Yeast Vacuolar H+-ATPase Is an Unconventional Glucose-Induced Effect
TLDR
It is proposed that glucose effects on V-ATPase assembly occur by a novel mechanism that requires glucose metabolism beyond formation of glucose 6-phosphate and generates a signal that can be sensed efficiently only by a catalytically competent V- ATPase.
Vacuolar and plasma membrane proton-adenosinetriphosphatases.
TLDR
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.
The RAVE Complex Is Essential for Stable Assembly of the Yeast V-ATPase*
TLDR
Evidence supporting a role for RAVE in reassembly of the V-ATPase is provided but also an essential role in V- ATPase assembly under other conditions is demonstrated.
Early Steps in Assembly of the Yeast Vacuolar H+-ATPase*
TLDR
The data suggest that in wild-type cells, assembly occurs predominantly by the concerted assembly pathway, and V-ATPase complexes acquire the full complement of Vosubunits during or after exit from the endoplasmic reticulum.
Structure and regulation of insect plasma membrane H(+)V-ATPase.
TLDR
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.
Disassembly and reassembly of the yeast vacuolar H(+)-ATPase in vivo.
  • P. Kane
  • Biology
    The Journal of biological chemistry
  • 1995
Partial assembly of the yeast vacuolar H(+)-ATPase in mutants lacking one subunit of the enzyme.
TLDR
Results indicate that the peripheral (V1) sector and integral membrane sectors of the yeast vacuolar H(+)-ATPase can assemble independently and can assemble into a complex in the absence of the 42-kDa peripheral subunit.
...
1
2
3
4
5
...