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| Title | Structural comparison of the vacuolar and Golgi V-ATPases from . |
|---|---|
| Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 116, Issue 15, Page 7272-7277, Year 2019 |
| Publish date | Apr 9, 2019 |
 Authors | Thamiya Vasanthakumar / Stephanie A Bueler / Di Wu / Victoria Beilsten-Edmands / Carol V Robinson / John L Rubinstein /   |
| PubMed Abstract | Proton-translocating vacuolar-type ATPases (V-ATPases) are necessary for numerous processes in eukaryotic cells, including receptor-mediated endocytosis, protein maturation, and lysosomal ...Proton-translocating vacuolar-type ATPases (V-ATPases) are necessary for numerous processes in eukaryotic cells, including receptor-mediated endocytosis, protein maturation, and lysosomal acidification. In mammals, V-ATPase subunit isoforms are differentially targeted to various intracellular compartments or tissues, but how these subunit isoforms influence enzyme activity is not clear. In the yeast , isoform diversity is limited to two different versions of the proton-translocating subunit a: Vph1p, which is targeted to the vacuole, and Stv1p, which is targeted to the Golgi apparatus and endosomes. We show that purified V-ATPase complexes containing Vph1p have higher ATPase activity than complexes containing Stv1p and that the relative difference in activity depends on the presence of lipids. We also show that V complexes containing Stv1p could be readily purified without attached V regions. We used this effect to determine structures of the membrane-embedded V region with Stv1p at 3.1-Å resolution, which we compare with a structure of the V region with Vph1p that we determine to 3.2-Å resolution. These maps reveal differences in the surface charge near the cytoplasmic proton half-channel. Both maps also show the presence of bound lipids, as well as regularly spaced densities that may correspond to ergosterol or bound detergent, around the c-ring. |
 External links | Proc Natl Acad Sci U S A / PubMed:30910982 / PubMed Central |
| Methods | EM (single particle) |
| Resolution | 3.1 - 8.7 Å |
| Structure data | EMDB-0644, PDB-6o7t: EMDB-0645, PDB-6o7u: EMDB-0646, PDB-6o7v: |
| Source |
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 Keywords | MEMBRANE PROTEIN / Proton pump |
saccharomyces cerevisiae (brewer's yeast)