VMA12 Encodes a Yeast Endoplasmic Reticulum Protein Required for Vacuolar H+-ATPase Assembly*

@article{Jackson1997VMA12EA,
  title={VMA12 Encodes a Yeast Endoplasmic Reticulum Protein Required for Vacuolar H+-ATPase Assembly*},
  author={D. Dewaine Jackson and Tom H. Stevens},
  journal={The Journal of Biological Chemistry},
  year={1997},
  volume={272},
  pages={25928 - 25934}
}
The Saccharomyces cerevisiae vacuolar membrane proton-translocating ATPase (V-ATPase) can be divided into a peripheral membrane complex (V1) containing at least eight polypeptides of 69, 60, 54, 42, 32, 27, 14, and 13 kDa, and an integral membrane complex (V0) containing at least five polypeptides of 100, 36, 23, 17, and 16 kDa. Other yeast genes have been identified that are required for V-ATPase assembly but whose protein products do not co-purify with the enzyme complex. One such gene,VMA12… 

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TLDR
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References

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Vma22p Is a Novel Endoplasmic Reticulum-associated Protein Required for Assembly of the Yeast Vacuolar H+-ATPase Complex (*)
TLDR
Results indicate that Vma22p, along with Vma21p and Vma12p, form a set of ER proteins required for V-ATPase assembly, which is associated with ER membranes.
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TLDR
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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.
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