Gene Symbol: VMA8
Description: H(+)-transporting V1 sector ATPase subunit D
Alias: H(+)-transporting V1 sector ATPase subunit D
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. Zhang Z, Zheng Y, Mazon H, Milgrom E, Kitagawa N, Kish Trier E, et al. Structure of the yeast vacuolar ATPase. J Biol Chem. 2008;283:35983-95 pubmed publisher
  2. Diab H, Ohira M, Liu M, Cobb E, Kane P. Subunit interactions and requirements for inhibition of the yeast V1-ATPase. J Biol Chem. 2009;284:13316-25 pubmed publisher
    ..We propose that upon disassembly, the H subunit undergoes a conformational change that inhibits V(1)-ATPase activity and precludes V(0) interactions. ..
  3. Diepholz M, Venzke D, Prinz S, Batisse C, Flörchinger B, Rössle M, et al. A different conformation for EGC stator subcomplex in solution and in the assembled yeast V-ATPase: possible implications for regulatory disassembly. Structure. 2008;16:1789-98 pubmed publisher
    ..However, the relative arrangement of the EG and C subunits in solution is more open than that in the holoenzyme, suggesting a conformational change of EGC during regulatory assembly and disassembly. ..
  4. Tomashek J, Garrison B, Klionsky D. Reconstitution in vitro of the V1 complex from the yeast vacuolar proton-translocating ATPase. Assembly recapitulates mechanism. J Biol Chem. 1997;272:16618-23 pubmed
    ..From these data, we extend our previous model to consider an assembly pathway whose steps reflect the catalytic mechanism of the Boyer binding-change model. ..
  5. Ohira M, Smardon A, Charsky C, Liu J, Tarsio M, Kane P. The E and G subunits of the yeast V-ATPase interact tightly and are both present at more than one copy per V1 complex. J Biol Chem. 2006;281:22752-60 pubmed
    ..J. (1997) J. Biol. Chem. 272, 26787-26793). These results are consistent with recent models showing at least two peripheral stalks connecting the V1 and V0 sectors of the V-ATPase and would allow both stalks to be based on an EG dimer. ..
  6. Zhang Z, Charsky C, Kane P, Wilkens S. Yeast V1-ATPase: affinity purification and structural features by electron microscopy. J Biol Chem. 2003;278:47299-306 pubmed
    ..Vasilyeva, E., and Forgac, M. (1999) J. Biol. Chem. 274, 31804-31810) indicates that the structure of the isolated V1 from yeast is very similar to the structure of the V1 domain in the intact V-ATPase complex. ..
  7. Keenan Curtis K, Kane P. Novel vacuolar H+-ATPase complexes resulting from overproduction of Vma5p and Vma13p. J Biol Chem. 2002;277:2716-24 pubmed
    ..Overproduced Vma5p associated with cytosolic V(1) complexes; this association may cause the lethality. ..
  8. Kawasaki Nishi S, Bowers K, Nishi T, Forgac M, Stevens T. The amino-terminal domain of the vacuolar proton-translocating ATPase a subunit controls targeting and in vivo dissociation, and the carboxyl-terminal domain affects coupling of proton transport and ATP hydrolysis. J Biol Chem. 2001;276:47411-20 pubmed
    ..Our results suggest that whereas targeting and in vivo dissociation are controlled by sequences located in the amino-terminal domains of the subunit a isoforms, coupling efficiency is controlled by the carboxyl-terminal region. ..
  9. Stevens T, Forgac M. Structure, function and regulation of the vacuolar (H+)-ATPase. Annu Rev Cell Dev Biol. 1997;13:779-808 pubmed
    ..Recent information concerning targeting and regulation of V-ATPases has also been obtained. ..

More Information


  1. Parsons L, Wilkens S. Probing subunit-subunit interactions in the yeast vacuolar ATPase by peptide arrays. PLoS ONE. 2012;7:e46960 pubmed publisher
    ..The subunit-subunit interaction data are discussed in context of our current model of reversible enzyme dissociation. ..
  2. Arata Y, Baleja J, Forgac M. Localization of subunits D, E, and G in the yeast V-ATPase complex using cysteine-mediated cross-linking to subunit B. Biochemistry. 2002;41:11301-7 pubmed
    ..Subunit D is thus the most likely homologue to the gamma subunit of F(1), which undergoes rotation during ATP hydrolysis and serves an essential function in rotary catalysis. ..
  3. Owegi M, Pappas D, Finch M, Bilbo S, Resendiz C, Jacquemin L, et al. Identification of a domain in the V0 subunit d that is critical for coupling of the yeast vacuolar proton-translocating ATPase. J Biol Chem. 2006;281:30001-14 pubmed
    ..Structural features conserved between bacterial and eukaryotic subunit d and the significance of domain 3 for vacuolar proton-translocating ATPase function are discussed. ..
  4. Rizzo J, Tarsio M, Martínez Muñoz G, Kane P. Diploids heterozygous for a vma13Delta mutation in Saccharomyces cerevisiae highlight the importance of V-ATPase subunit balance in supporting vacuolar acidification and silencing cytosolic V1-ATPase activity. J Biol Chem. 2007;282:8521-32 pubmed
    ..The results suggest that balancing levels of subunit H with those of other V-ATPase subunits is critical, both for allowing organelle acidification and for preventing unproductive hydrolysis of cytosolic ATP. ..
  5. Thaker Y, Roessle M, Gruber G. The boxing glove shape of subunit d of the yeast V-ATPase in solution and the importance of disulfide formation for folding of this protein. J Bioenerg Biomembr. 2007;39:275-89 pubmed
    ..Cysteins, involved in disulfide bridges, were analyzed by MALDI-TOF mass spectrometry. Finally, the solution structure of subunit d will be discussed in terms of the topological arrangement of the V(1)V(O) ATPase. ..
  6. Tomashek J, Graham L, Hutchins M, Stevens T, Klionsky D. V1-situated stalk subunits of the yeast vacuolar proton-translocating ATPase. J Biol Chem. 1997;272:26787-93 pubmed
    ..This may be important in the regulation of assembly, since these two subunits add to the V1 during later stages of V1 assembly. This is the first demonstration of interdependence between ATPase subunits for structural stability. ..
  7. Tomashek J, Sonnenburg J, Artimovich J, Klionsky D. Resolution of subunit interactions and cytoplasmic subcomplexes of the yeast vacuolar proton-translocating ATPase. J Biol Chem. 1996;271:10397-404 pubmed
    ..All larger complexes are lost in the Deltavma1, Deltavma2, and Deltavma8 strains. We designate the large complex seen in wild-type cells containing at least subunits Vma1p, Vma2p, Vma4p, Vma7p, and Vma8p as the definitive V1 complex. ..
  8. Balakrishna A, Basak S, Manimekalai M, Grüber G. Crystal structure of subunits D and F in complex gives insight into energy transmission of the eukaryotic V-ATPase from Saccharomyces cerevisiae. J Biol Chem. 2015;290:3183-96 pubmed publisher
    ..Furthermore, the flexibility of the terminal helices of both subunits as well as the loop (26)GQITPETQEK(35) provides information about the regulatory step of reversible V1VO disassembly. ..
  9. Oluwatosin Y, Kane P. Mutations in the yeast KEX2 gene cause a Vma(-)-like phenotype: a possible role for the Kex2 endoprotease in vacuolar acidification. Mol Cell Biol. 1998;18:1534-43 pubmed
    ..This is the first time a mutation of this type has been identified. ..
  10. Ghavidel A, Baxi K, Ignatchenko V, Prusinkiewicz M, Arnason T, Kislinger T, et al. A Genome Scale Screen for Mutants with Delayed Exit from Mitosis: Ire1-Independent Induction of Autophagy Integrates ER Homeostasis into Mitotic Lifespan. PLoS Genet. 2015;11:e1005429 pubmed publisher
    ..Our data provide evidence that catabolism of protein aggregates, a natural byproduct of high protein synthesis and turn over in dividing cells, is among the drivers of mitotic longevity in eukaryotes. ..