Gene Symbol: VMA13
Description: H(+)-transporting V1 sector ATPase subunit H
Alias: CLS11, H(+)-transporting V1 sector ATPase subunit H
Species: Saccharomyces cerevisiae S288c

Top Publications

  1. 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. ..
  2. 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
  3. 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. ..
  4. Landolt Marticorena C, Williams K, Correa J, Chen W, Manolson M. Evidence that the NH2 terminus of vph1p, an integral subunit of the V0 sector of the yeast V-ATPase, interacts directly with the Vma1p and Vma13p subunits of the V1 sector. J Biol Chem. 2000;275:15449-57 pubmed
    ..These results suggest that Vph1p may function as a component of a fixed structural link, or stator, coupling V(1) ATP hydrolysis to V(0) proton translocation. ..
  5. Oot R, Wilkens S. Domain characterization and interaction of the yeast vacuolar ATPase subunit C with the peripheral stator stalk subunits E and G. J Biol Chem. 2010;285:24654-64 pubmed publisher
    ..Our findings indicate that the high affinity site for EGC interaction is C(head). In addition, we provide evidence that the EGC(head) interaction greatly stabilizes EG heterodimer. ..
  6. 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. ..
  7. 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. ..
  8. 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. ..
  9. Jefferies K, Forgac M. Subunit H of the vacuolar (H+) ATPase inhibits ATP hydrolysis by the free V1 domain by interaction with the rotary subunit F. J Biol Chem. 2008;283:4512-9 pubmed
    ..These results indicate that subunits H and F are proximal in free V1, supporting the hypothesis that subunit H inhibits free V1 by bridging the rotary and stator domains. ..

More Information


  1. Lu M, Vergara S, Zhang L, Holliday L, Aris J, Gluck S. The amino-terminal domain of the E subunit of vacuolar H(+)-ATPase (V-ATPase) interacts with the H subunit and is required for V-ATPase function. J Biol Chem. 2002;277:38409-15 pubmed
    ..Our data demonstrate the physiological significance of the interaction between the E and H subunits of V-ATPase and extend previous studies on the arrangement of subunits on the peripheral stalk of V-ATPase. ..
  2. 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. ..
  3. Li S, Diakov T, Rizzo J, Kane P. Vacuolar H+-ATPase works in parallel with the HOG pathway to adapt Saccharomyces cerevisiae cells to osmotic stress. Eukaryot Cell. 2012;11:282-91 pubmed publisher
    ..Together, these data suggest that the V-ATPase acts in parallel with the HOG pathway in order to mediate salt detoxification. ..
  4. Lafourcade C, Galan J, Gloor Y, Haguenauer Tsapis R, Peter M. The GTPase-activating enzyme Gyp1p is required for recycling of internalized membrane material by inactivation of the Rab/Ypt GTPase Ypt1p. Mol Cell Biol. 2004;24:3815-26 pubmed
    ..Interestingly, the deletions of GYP1 and YPT6 were synthetic lethal, raising the possibility that at least two distinct pathways are involved in recycling of membrane material. ..
  5. 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. ..
  6. 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 V-ATPase H subunit (encoded by the VMA13 gene) activates ATP-driven proton pumping in intact V-ATPase complexes and inhibits MgATPase activity in cytosolic V1 sectors (Parra, K. J., Keenan, K. L., and Kane, P. M. (2000) J. Biol. Chem...
  7. Lin M, Li S, Kane P, Höfken T. Regulation of vacuolar H+-ATPase activity by the Cdc42 effector Ste20 in Saccharomyces cerevisiae. Eukaryot Cell. 2012;11:442-51 pubmed publisher
    ..Using the split-ubiquitin technique, we found that Ste20 forms a complex with Vma13, an important regulatory subunit of vacuolar H(+)-ATPase (V-ATPase)...
  8. Benlekbir S, Bueler S, Rubinstein J. Structure of the vacuolar-type ATPase from Saccharomyces cerevisiae at 11-Å resolution. Nat Struct Mol Biol. 2012;19:1356-62 pubmed publisher
    ..We provide support for this model by demonstrating that mutation of subunit H to increase the rigidity of the linker between its two domains decreases its ability to inhibit ATPase activity. ..
  9. Matsumoto R, Suzuki K, Ohya Y. Organelle acidification is important for localisation of vacuolar proteins in Saccharomyces cerevisiae. Protoplasma. 2013;250:1283-93 pubmed publisher
    ..These results suggest that many alterations in the localisation of vacuolar proteins occur after loss of the acidification of acidic compartments. ..
  10. Flannery A, Stevens T. Functional characterization of the N-terminal domain of subunit H (Vma13p) of the yeast vacuolar ATPase. J Biol Chem. 2008;283:29099-108 pubmed publisher
    ..One of the regulatory subunits, subunit H, is encoded by the VMA13 gene in yeast and is composed of two domains, the N-terminal domain (amino acids (aa) 1-352) and the C-terminal ..
  11. 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. ..
  12. 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. ..
  13. Zhong X, Malhotra R, Guidotti G. Regulation of yeast ectoapyrase ynd1p activity by activator subunit Vma13p of vacuolar H+-ATPase. J Biol Chem. 2000;275:35592-9 pubmed
    ..ADPase activity of Ynd1p in a vma13Delta mutant was drastically increased compared with that of Ynd1p in VMA13 cells...
  14. 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. ..
  15. Lin Z, Dong M, Zhang Y, Lee E, Lin H. Cbr1 is a Dph3 reductase required for the tRNA wobble uridine modification. Nat Chem Biol. 2016;12:995-997 pubmed publisher
    ..The NADH- and Cbr1-dependent reduction of Dph3 may provide a regulatory linkage between cellular metabolic state and protein translation. ..