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STV1  -  H(+)-transporting V0 sector ATPase subunit a

Saccharomyces cerevisiae S288c

Synonyms: V-ATPase 101 kDa subunit, V-ATPase a 2 subunit, V-ATPase subunit AC115, V-type proton ATPase subunit a, Golgi isoform, Vacuolar proton translocating ATPase subunit a 2, ...
 
 
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High impact information on STV1

  • The a4 W520L mutation phenotypes were dominant negative, as overexpression of wild type yeast a isoforms, Vph1p, or Stv1p, did not restore growth [1].
  • The Vph1p-containing complex localizes to the vacuole, whereas the Stv1p-containing complex resides in some other intracellular compartment, suggesting that the a subunit contains information necessary for the correct targeting of the V-ATPase [2].
  • We also compared the ability of V-ATPase complexes containing Vph1p or Stv1p to undergo in vivo dissociation in response to glucose depletion [3].
  • Interestingly, the V-ATPase complex containing the chimera with the carboxyl-terminal domain of Vph1p exhibited a higher coupling of proton transport to ATP hydrolysis than the chimera containing the carboxyl-terminal domain of Stv1p [2].
  • Vph1p localizes to the central vacuole, whereas Stv1p is present in some other compartment, possibly the Golgi or endosomes [3].
 

Biological context of STV1

 

Anatomical context of STV1

  • Immunological assays of sucrose gradient fractions revealed that the amount of Stv1p was elevated in the vph1 triangle up strain, and that vacuoles purified by this method with no detectable endosomal contamination contain an assembled V-ATPase complex, but with much lower activity than the wild type [4].
  • We show that Stv1p localizes to a late Golgi compartment at steady state and cycles continuously via a prevacuolar endosome back to the Golgi [2].
 

Physical interactions of STV1

  • Complexes containing Stv1p showed lower assembly with the peripheral V(1) domain than did complexes containing Vph1p [3].
 

Other interactions of STV1

  • Subunit a of V-ATPase in the yeast Saccharomyces cerevisiae, in contrast to its other subunits, is encoded by two genes VPH1 and STV1 [4].
  • We demonstrate that disruption of yeast VMA9 results in the failure of V1 and V0 V-ATPase subunits to assemble onto the vacuole and in decreased levels of the subunit a isoforms Vph1p and Stv1p [5].

References

  1. Effects of human a3 and a4 mutations that result in osteopetrosis and distal renal tubular acidosis on yeast V-ATPase expression and activity. Ochotny, N., Van Vliet, A., Chan, N., Yao, Y., Morel, M., Kartner, N., von Schroeder, H.P., Heersche, J.N., Manolson, M.F. J. Biol. Chem. (2006) [Pubmed]
  2. 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. Kawasaki-Nishi, S., Bowers, K., Nishi, T., Forgac, M., Stevens, T.H. J. Biol. Chem. (2001) [Pubmed]
  3. Yeast V-ATPase complexes containing different isoforms of the 100-kDa a-subunit differ in coupling efficiency and in vivo dissociation. Kawasaki-Nishi, S., Nishi, T., Forgac, M. J. Biol. Chem. (2001) [Pubmed]
  4. Characterization of yeast V-ATPase mutants lacking Vph1p or Stv1p and the effect on endocytosis. Perzov, N., Padler-Karavani, V., Nelson, H., Nelson, N. J. Exp. Biol. (2002) [Pubmed]
  5. Vma9p (subunit e) is an integral membrane V0 subunit of the yeast V-ATPase. Compton, M.A., Graham, L.A., Stevens, T.H. J. Biol. Chem. (2006) [Pubmed]
 
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