V-ATPase
Sign in to saveAlso known as Vacuolar-type H+-ATPase, V-type ATPase, V1V0-ATPase, Vacuolar Proton-Translocating ATPases, Vacuolar Proton-Translocating ATPase, Vacuolar-type adenosine triphosphatase
Vacuolar-type ATPase (V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms. V-ATPases acidify a wide array of intracellular organelles and pump protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however, is a proton pump that
Research
3,301 papers- V-ATPase in cancer: mechanistic insights and therapeutic potentials.Cell communication and signaling : CCS · 2024
- The Plant V-ATPase.Frontiers in plant science · 2022
- The V-ATPase/ATG16L1 axis is controlled by the V(1)H subunit.Molecular cell · 2024
- A Bacterial Effector Reveals the V-ATPase-ATG16L1 Axis that Initiates Xenophagy.Cell · 2019
- Bafilomycin A1 disrupts autophagic flux by inhibiting both V-ATPase-dependent acidification and Ca-P60A/SERCA-dependent autophagosome-lysosome fusion.Autophagy · 2015
via PubMed
~17 min read
Article
22 sectionsContents
- Roles played by V-ATPases
- Structure
- V<sub>1</sub>
- Subunit C
- Subunit C function
- Subunits E, G
- Subunit H
- V<sub>o</sub>
- Subunit a/I
- Subunit d/C
- Subunit c
- V-ATPase assembly
- V-ATPase evolution
- Regulation of V-ATPase activity
- Human diseases
- Osteopetrosis
- Distal renal tubular acidosis (dRTA)
- X-linked myopathy with excessive autophagy (XMEA)
- Nomenclature
- See also
- References
- External links
Vacuolar-type ATPase (V-ATPase) is a highly conserved evolutionarily ancient enzyme with remarkably diverse functions in eukaryotic organisms. V-ATPases acidify a wide array of intracellular organelles and pump protons across the plasma membranes of numerous cell types. V-ATPases couple the energy of ATP hydrolysis to proton transport across intracellular and plasma membranes of eukaryotic cells. It is generally seen as the polar opposite of ATP synthase because ATP synthase is a proton channel that uses the energy from a proton gradient to produce ATP. V-ATPase however, is a proton pump that uses the energy from ATP hydrolysis to produce a proton gradient.
The Archaea-type ATPase (A-ATPase) is a related group of ATPases found in archaea that often work as an ATP synthase. It forms a clade V/A-ATPase with V-ATPase. Most members of either group shuttle protons (), but a few members have evolved to use sodium ions () instead.