VMA8/YEL051W Summary Help

VMA8 BASIC INFORMATION

Standard Name VMA8
Systematic Name YEL051W
Feature Type ORF, Verified
Description Subunit D of the eight-subunit V1 peripheral membrane domain of the vacuolar H+-ATPase (V-ATPase), an electrogenic proton pump found throughout the endomembrane system; plays a role in the coupling of proton transport and ATP hydrolysis (1, 2, 3 and see Summary Paragraph)
Name Description Vacuolar Membrane Atpase
GO Annotations All VMA8 GO evidence and references
    View Computational GO annotations for VMA8
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Mutant Phenotype All VMA8 Phenotype details and references
Classical genetics
null
Large-scale survey
null
Interactions VMA8 All interactions details and references
82 total interaction(s) for 50 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 35
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 7
  • Co-fractionation: 5
  • Co-purification: 1
  • PCA: 18
  • Two-hybrid: 5
Genetic Interactions
  • Synthetic Growth Defect: 6
  • Synthetic Haploinsufficiency: 1
  • Synthetic Lethality: 3
Sequence Information
ChrV:58378 to 59148 | ORF Map | GBrowse
Gbrowse
Last Update Coordinates: 1996-07-31 | Sequence: 1996-07-31
Subfeature details
Relative
Coordinates		 Chromosomal
Coordinates		 Most Recent Updates
Coordinates Sequence
CDS 1..771 58378..59148 1996-07-31 1996-07-31
External Links All Associated Seq | E.C. | Entrez Gene | Entrez RefSeq Protein | MIPS | UniProtKB
Primary SGDIDS000000777

VMA8 RESOURCES

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Expression Summary histogram

ADDITIONAL INFORMATION for VMA8

SUMMARY PARAGRAPH for VMA8

VMA8 encodes the D subunit of the yeast V-ATPase V1 domain (1, 4). Vacuolar (H )-ATPases (V-ATPases) are ATP-dependent proton pumps that acidify intracellular vacuolar compartments. Vacuolar acidification is important for many cellular processes, including endocytosis, targeting of newly synthesized lysosomal enzymes, and other molecular targeting processes. The V-ATPase consists of two separable domains. The V1 domain has eight known subunits, is peripherally associated with the vacuolar membrane, and catalyzes ATP hydrolysis. The V0 domain is an integral membrane structure of five subunits, and transports protons across the membrane. The structure, function, and assembly of V-ATPases are reviewed in references 3, 5, 6 and 7.

The vma8 null mutant is viable but lacks vacuolar (H )-ATPase activity, cannot grow at neutral pH or on nonfermentable carbon sources, and fails to accumulate quinacrine in the vacuole (1, 4). In the absence of Vma8p, the remaining V1 subunits do not associate with the vacuolar membrane (1). A specific interaction between Vma8p and the V-ATPase F subunit (Vma7p) has been detected (8). Several mutations in VMA8 cause uncoupling of proton transport from ATPase activity, suggesting that the D subunit normally plays an important role in coupling these activities (2).

V-ATPases have been identified in numerous eukaryotes (3, 7); a bovine cDNA encoding a homolog of the V-ATPase D subunit has been cloned (4).

Last updated: 2000-05-15

REFERENCES CITED ON THIS PAGE [View Complete Literature Guide for VMA8]

1) Graham LA, et al.  (1995) VMA8 encodes a 32-kDa V1 subunit of the Saccharomyces cerevisiae vacuolar H(+)-ATPase required for function and assembly of the enzyme complex. J Biol Chem 270(25):15037-44
2) Xu T and Forgac M  (2000) Subunit D (Vma8p) of the yeast vacuolar H+-ATPase plays a role in coupling of proton transport and ATP hydrolysis. J Biol Chem 275(29):22075-81
3) Forgac M  (1999) Structure and properties of the vacuolar (H+)-ATPases. J Biol Chem 274(19):12951-4
4) Nelson H, et al.  (1995) A bovine cDNA and a yeast gene (VMA8) encoding the subunit D of the vacuolar H(+)-ATPase. Proc Natl Acad Sci U S A 92(2):497-501
5) Graham LA and Stevens TH  (1999) Assembly of the yeast vacuolar proton-translocating ATPase. J Bioenerg Biomembr 31(1):39-47
6) Kane PM  (1999) Biosynthesis and regulation of the yeast vacuolar H+-ATPase. J Bioenerg Biomembr 31(1):49-56
7) Stevens TH and Forgac M  (1997) Structure, function and regulation of the vacuolar (H+)-ATPase. Annu Rev Cell Dev Biol 13:779-808
8) Tomashek JJ, et al.  (1997) V1-situated stalk subunits of the yeast vacuolar proton-translocating ATPase. J Biol Chem 272(42):26787-93