Vma22p Is a Novel Endoplasmic Reticulum-associated Protein Required for Assembly of the Yeast Vacuolar H+-ATPase Complex (*)

@article{Hill1995Vma22pIA,
  title={Vma22p Is a Novel Endoplasmic Reticulum-associated Protein Required for Assembly of the Yeast Vacuolar H+-ATPase Complex (*)},
  author={Kathryn J. Hill and Tom H. Stevens},
  journal={The Journal of Biological Chemistry},
  year={1995},
  volume={270},
  pages={22329 - 22336}
}
  • K. Hill, T. Stevens
  • Published 22 September 1995
  • Biology, Chemistry
  • The Journal of Biological Chemistry
The Saccharomyces cerevisiae vacuolar H-ATPase (V-ATPase) is a multi-subunit complex that can be structurally and functionally divided into peripheral (V) and integral membrane (V) sectors. The vma22-1 mutation was isolated in a screen for mutants defective in V-ATPase function. vma22Δ cells contain no V-ATPase activity due to a failure to assemble the enzyme complex; V subunits accumulate in the cytosol, and the V 100-kDa subunit is rapidly degraded. Turnover of the 100-kDa integral membrane… 
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VMA12 Encodes a Yeast Endoplasmic Reticulum Protein Required for Vacuolar H+-ATPase Assembly*
TLDR
Data indicate that Vma12p functions in the ER after the insertion of V0subunits into the ER membrane, and that assembly is required for the stability of the V0 subunits and their transport as a complex out of this compartment.
Vma9p (Subunit e) Is an Integral Membrane V0 Subunit of the Yeast V-ATPase*
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It is demonstrated that disruption of yeast VMA9 results in the failure of V1 and V0 V-ATPase subunits to assemble onto the vacuole and in decreased levels of the subunit a isoforms Vph1p and Stv1p, and suggested a model for the arrangement of polypeptides within the V0 subcomplex.
Assembly of the Yeast Vacuolar H+-ATPase Occurs in the Endoplasmic Reticulum and Requires a Vma12p/Vma22p Assembly Complex
TLDR
Subcellular fractionation and chemical cross-linking studies have revealed that Vma12p and Vma22p form a stable membrane associated complex, the first evidence for a dedicated assembly complex in the ER required for the assembly of an integral membrane protein complex (V-ATPase) as it is transported through the secretory pathway.
Role of Vma21p in assembly and transport of the yeast vacuolar ATPase.
TLDR
It is concluded that Vma21p is not involved in regulating the interaction between V0 and V1 sectors, but that it has a crucial role in coordinating the assembly of V0 subunits and in escorting the assembled V0 complex into ER-derived transport vesicles.
VMA11 and VMA16 Encode Second and Third Proteolipid Subunits of the Saccharomyces cerevisiae Vacuolar Membrane H+-ATPase*
TLDR
Results suggest that the three proteolipid subunits of the V-ATPase have similar but not redundant functions, each of which is most likely involved in proton transport activity of the enzyme complex.
Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum.
TLDR
A fifth V(0) assembly factor is discovered, Voa1p (YGR106C); an endoplasmic reticulum (ER)-localized integral membrane glycoprotein whose role was revealed in cells expressing an ER retrieval-deficient form of the V-ATPase assembly factor Vma21p (Vma 21pQQ).
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.
Assembly of the Yeast Vacuolar Proton-Translocating ATPase
TLDR
Three genes in yeast are identified that codefor proteins that are not part of the final V-ATPase complex yet required for its assembly, and these nonsubunit Vma proteins are referred to as assembly factors, since their function is dedicated to assembling the V- ATPase.
Structure and Assembly of the Yeast V-ATPase
TLDR
The yeast V-ATPase belongs to a family of V-type ATPases present in all eucaryotic organisms and homologues of the Vma21p assembly factor have been identified in many higher eukaryotes supporting a ubiquitous assembly pathway for this important enzyme complex.
Sorting of the Yeast Vacuolar-type, Proton-translocating ATPase Enzyme Complex (V-ATPase)
TLDR
A structural model is proposed of the intact Stv1p-containing V-ATPase demonstrating the accessibility of the W83KY sequence to retrograde sorting machinery, and defines a novel sorting signal that is both necessary and sufficient for trafficking of the V- ATPase within the Golgi/endosomal network.
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References

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TLDR
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VMA7 encodes a novel 14-kDa subunit of the Saccharomyces cerevisiae vacuolar H(+)-ATPase complex.
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TLDR
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The 31-kDa polypeptide is an essential subunit of the vacuolar ATPase in Saccharomyces cerevisiae.
  • F. Foury
  • Biology
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  • 1990
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