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Structural comparison of the vacuolar and Golgi V-ATPases from Saccharomyces cerevisiae.

Vasanthakumar T, Bueler SA, Wu D, Beilsten-Edmands V, Robinson CV, Rubinstein JL
Proc Natl Acad Sci U S A 116 7272-7277 (2019)
Related entries: 6o7t, 6o7u, 6o7v, 6o7w

Cited: 37 times
EuropePMC logo PMID: 30910982

Abstract

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 Saccharomyces cerevisiae, 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 VO complexes containing Stv1p could be readily purified without attached V1 regions. We used this effect to determine structures of the membrane-embedded VO region with Stv1p at 3.1-Å resolution, which we compare with a structure of the VO 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.

Articles - 6o7x mentioned but not cited (1)

  1. Structural comparison of the vacuolar and Golgi V-ATPases from Saccharomyces cerevisiae. Vasanthakumar T, Bueler SA, Wu D, Beilsten-Edmands V, Robinson CV, Rubinstein JL. Proc Natl Acad Sci U S A 116 7272-7277 (2019)


Reviews citing this publication (7)

  1. Regulation and function of V-ATPases in physiology and disease. Collins MP, Forgac M. Biochim Biophys Acta Biomembr 1862 183341 (2020)
  2. Regulation of V-ATPase Activity and Organelle pH by Phosphatidylinositol Phosphate Lipids. Banerjee S, Kane PM. Front Cell Dev Biol 8 510 (2020)
  3. The V-ATPases in cancer and cell death. Chen F, Kang R, Liu J, Tang D. Cancer Gene Ther 29 1529-1541 (2022)
  4. The V-ATPase a3 Subunit: Structure, Function and Therapeutic Potential of an Essential Biomolecule in Osteoclastic Bone Resorption. Chu A, Zirngibl RA, Manolson MF. Int J Mol Sci 22 6934 (2021)
  5. The Plant V-ATPase. Seidel T. Front Plant Sci 13 931777 (2022)
  6. Structural and Functional Diversity of Two ATP-Driven Plant Proton Pumps. Kabała K, Janicka M. Int J Mol Sci 24 4512 (2023)
  7. The cytosolic N-terminal domain of V-ATPase a-subunits is a regulatory hub targeted by multiple signals. Tuli F, Kane PM. Front Mol Biosci 10 1168680 (2023)

Articles citing this publication (29)

  1. Structure of V-ATPase from the mammalian brain. Abbas YM, Wu D, Bueler SA, Robinson CV, Rubinstein JL. Science 367 1240-1246 (2020)
  2. Structure of mycobacterial ATP synthase bound to the tuberculosis drug bedaquiline. Guo H, Courbon GM, Bueler SA, Mai J, Liu J, Liu J, Rubinstein JL. Nature 589 143-147 (2021)
  3. Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly. Wang L, Wu D, Robinson CV, Wu H, Fu TM. Mol Cell 80 501-511.e3 (2020)
  4. Cryo-EM structures provide insight into how E. coli F1Fo ATP synthase accommodates symmetry mismatch. Sobti M, Walshe JL, Wu D, Ishmukhametov R, Zeng YC, Robinson CV, Berry RM, Stewart AG. Nat Commun 11 2615 (2020)
  5. Structure of a mitochondrial ATP synthase with bound native cardiolipin. Mühleip A, McComas SE, Amunts A. Elife 8 e51179 (2019)
  6. Molecular basis of V-ATPase inhibition by bafilomycin A1. Wang R, Wang J, Hassan A, Lee CH, Xie XS, Li X. Nat Commun 12 1782 (2021)
  7. Cryo-EM and MD infer water-mediated proton transport and autoinhibition mechanisms of Vo complex. Roh SH, Shekhar M, Pintilie G, Chipot C, Wilkens S, Singharoy A, Chiu W. Sci Adv 6 eabb9605 (2020)
  8. Molecular basis of cholesterol efflux via ABCG subfamily transporters. Sun Y, Wang J, Long T, Qi X, Donnelly L, Elghobashi-Meinhardt N, Esparza L, Cohen JC, Xie XS, Hobbs HH, Li X. Proc Natl Acad Sci U S A 118 e2110483118 (2021)
  9. Structure of Ycf1p reveals the transmembrane domain TMD0 and the regulatory region of ABCC transporters. Bickers SC, Benlekbir S, Rubinstein JL, Kanelis V. Proc Natl Acad Sci U S A 118 e2025853118 (2021)
  10. Potassium and Sodium Salt Stress Characterization in the Yeasts Saccharomyces cerevisiae, Kluyveromyces marxianus, and Rhodotorula toruloides. Illarionov A, Lahtvee PJ, Kumar R. Appl Environ Microbiol 87 e0310020 (2021)
  11. The Arabidopsis V-ATPase is localized to the TGN/EE via a seed plant-specific motif. Lupanga U, Röhrich R, Askani J, Hilmer S, Kiefer C, Krebs M, Kanazawa T, Ueda T, Schumacher K. Elife 9 e60568 (2020)
  12. Detection and quantification of the vacuolar H+ATPase using the Legionella effector protein SidK. Maxson ME, Abbas YM, Wu JZ, Plumb JD, Grinstein S, Rubinstein JL. J Cell Biol 221 e202107174 (2022)
  13. High-throughput functional characterization of protein phosphorylation sites in yeast. Viéitez C, Busby BP, Ochoa D, Mateus A, Memon D, Galardini M, Yildiz U, Trovato M, Jawed A, Geiger AG, Oborská-Oplová M, Potel CM, Vonesch SC, Szu Tu C, Shahraz M, Stein F, Steinmetz LM, Panse VG, Noh KM, Savitski MM, Typas A, Beltrao P. Nat Biotechnol 40 382-390 (2022)
  14. Coordinated conformational changes in the V1 complex during V-ATPase reversible dissociation. Vasanthakumar T, Keon KA, Bueler SA, Jaskolka MC, Rubinstein JL. Nat Struct Mol Biol 29 430-439 (2022)
  15. Mechanical inhibition of isolated Vo from V/A-ATPase for proton conductance. Kishikawa JI, Nakanishi A, Furuta A, Kato T, Namba K, Tamakoshi M, Mitsuoka K, Yokoyama K. Elife 9 e56862 (2020)
  16. Ras-mutant cancers are sensitive to small molecule inhibition of V-type ATPases in mice. Tolani B, Celli A, Yao Y, Tan YZ, Fetter R, Liem CR, de Smith AJ, Vasanthakumar T, Bisignano P, Cotton AD, Seiple IB, Rubinstein JL, Jost M, Weissman JS. Nat Biotechnol 40 1834-1844 (2022)
  17. A distinct inhibitory mechanism of the V-ATPase by Vibrio VopQ revealed by cryo-EM. Peng W, Casey AK, Fernandez J, Carpinone EM, Servage KA, Chen Z, Li Y, Tomchick DR, Starai VJ, Orth K. Nat Struct Mol Biol 27 589-597 (2020)
  18. Plasma Membrane Protein Nce102 Modulates Morphology and Function of the Yeast Vacuole. Vaskovicova K, Vesela P, Zahumensky J, Folkova D, Balazova M, Malinsky J. Biomolecules 10 E1476 (2020)
  19. Toosendanin, a novel potent vacuolar-type H+-translocating ATPase inhibitor, sensitizes cancer cells to chemotherapy by blocking protective autophagy. Dong Y, Zhu G, Wang SF, Keon KA, Rubinstein JL, Zeng SX, Zhang S, Chen QL, Fu J, Li M, Shen HM, Lu JJ, Chen XP, Lu JH. Int J Biol Sci 18 2684-2702 (2022)
  20. Cholesterol efflux mechanism revealed by structural analysis of human ABCA1 conformational states. Sun Y, Li X. Nat Cardiovasc Res 1 238-245 (2022)
  21. Chimeric a-subunit isoforms generate functional yeast V-ATPases with altered regulatory properties in vitro and in vivo. Tuli F, Kane PM. Mol Biol Cell 34 ar14 (2023)
  22. CryoEM of endogenous mammalian V-ATPase interacting with the TLDc protein mEAK-7. Tan YZ, Abbas YM, Wu JZ, Wu D, Keon KA, Hesketh GG, Bueler SA, Gingras AC, Robinson CV, Grinstein S, Rubinstein JL. Life Sci Alliance 5 e202201527 (2022)
  23. Direct observation of stepping rotation of V-ATPase reveals rigid component in coupling between Vo and V1 motors. Otomo A, Iida T, Okuni Y, Ueno H, Murata T, Iino R. Proc Natl Acad Sci U S A 119 e2210204119 (2022)
  24. A Role for the V0 Sector of the V-ATPase in Neuroexocytosis: Exogenous V0d Blocks Complexin and SNARE Interactions with V0c. Lévêque C, Maulet Y, Wang Q, Rame M, Rodriguez L, Mochida S, Sangiardi M, Youssouf F, Iborra C, Seagar M, Vitale N, El Far O. Cells 12 750 (2023)
  25. Structural basis of V-ATPase VO region assembly by Vma12p, 21p, and 22p. Wang H, Bueler SA, Rubinstein JL. Proc Natl Acad Sci U S A 120 e2217181120 (2023)
  26. The Role of Sch9 and the V-ATPase in the Adaptation Response to Acetic Acid and the Consequences for Growth and Chronological Lifespan. Deprez MA, Maertens JM, Olsson L, Bettiga M, Winderickx J. Microorganisms 9 1871 (2021)
  27. Human V-ATPase a-subunit isoforms bind specifically to distinct phosphoinositide phospholipids. Mitra C, Winkley S, Kane PM. J Biol Chem 299 105473 (2023)
  28. Six states of Enterococcus hirae V-type ATPase reveals non-uniform rotor rotation during turnover. Burton-Smith RN, Song C, Ueno H, Murata T, Iino R, Murata K. Commun Biol 6 755 (2023)
  29. Yeast as a tool for membrane protein production and structure determination. Carlesso A, Delgado R, Ruiz Isant O, Uwangue O, Valli D, Bill RM, Hedfalk K. FEMS Yeast Res 22 foac047 (2022)


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