Wheat V-H+-ATPase subunit genes significantly affect salt tolerance in Arabidopsis thaliana. [PDF]
PLoS ONE, 2014 Genes for V-H(+)-ATPase subunits were identified and cloned from the salt-tolerant wheat mutant RH8706-49. Sequences of these genes are highly conserved in plants.
Xiaoliang He +3 more
doaj +1 more source
STING induces LC3B lipidation onto single-membrane vesicles via the V-ATPase and ATG16L1-WD40 domain
Journal of Cell Biology, 2020 A primordial function of the cGAS/STING pathway may be to induce LC3B lipidation. Fischer et al. show cGAMP-activated STING induces the V-ATPase to recruit ATG16L1 for lipidation of LC3B onto single-membrane perinuclear vesicles.
Tara D. Fischer +4 more
semanticscholar +1 more source
EMBO Journal, 2021 The vacuolar ATPase (V‐ATPase) is a rotary motor proton pump that is regulated by an assembly equilibrium between active holoenzyme and autoinhibited V1‐ATPase and Vo proton channel subcomplexes.
Md. Murad Khan +6 more
semanticscholar +1 more source
An extended nomenclature for mammalian V-ATPase subunit genes and splice variants. [PDF]
PLoS ONE, 2010 The vacuolar-type H(+)-ATPase (V-ATPase) is a multisubunit proton pump that is involved in both intra- and extracellular acidification processes throughout the body.
Kevin C Miranda +2 more
doaj +1 more source
The H+-ATPase (V-ATPase): from proton pump to signaling complex in health and disease
American Journal of Physiology - Cell Physiology, 2020 A primary function of the H+-ATPase (or V-ATPase) is to create an electrochemical proton gradient across eukaryotic cell membranes, which energizes fundamental cellular processes.
A. Eaton, M. Merkulova, Dennis Brown
semanticscholar +1 more source
V-ATPases and osteoclasts: ambiguous future of V-ATPases inhibitors in osteoporosis
Theranostics, 2018 Vacuolar ATPases (V-ATPases) play a critical role in regulating extracellular acidification of osteoclasts and bone resorption. The deficiencies of subunit a3 and d2 of V-ATPases result in increased bone density in humans and mice. One of the traditional drug design strategies in treating osteoporosis is the use of subunit a3 inhibitor. Recent findings
Tielin Yang +3 more
openaire +3 more sources
The Mechanochemistry of V-ATPase Proton Pumps [PDF]
Biophysical Journal, 2000 The vacuolar H(+)-ATPases (V-ATPases) are a universal class of proton pumps that are structurally similar to the F-ATPases. Both protein families are characterized by a membrane-bound segment (V(o), F(o)) responsible for the translocation of protons, and a soluble portion, (V(1), F(1)), which supplies the energy for translocation by hydrolyzing ATP ...
Hongyun Wang +2 more
openaire +3 more sources
Defining steps in RAVE-catalyzed V-ATPase assembly using purified RAVE and V-ATPase subcomplexes [PDF]
Journal of Biological Chemistry, 2021 The vacuolar H+-ATPase (V-ATPase) is a highly conserved proton pump responsible for the acidification of intracellular organelles in virtually all eukaryotic cells. V-ATPases are regulated by the rapid and reversible disassembly of the peripheral V1 domain from the integral membrane Vo domain, accompanied by release of the V1 C subunit from both ...
Michael C. Jaskolka +4 more
openaire +3 more sources
Estimating the Rotation Rate in the Vacuolar Proton-ATPase in Native Yeast Vacuolar Membranes [PDF]
, 2012 The rate of rotation of the rotor of the yeast vacuolar proton-ATPase (V-ATPase), relative to the stator or the steady parts of enzyme, is estimated in native vacuolar membrane vesicles of Saccharomyces cerevisiae under standardised conditions.
Bóta, A. +9 more
core +1 more source
Expansion of Thaumarchaeota habitat range is correlated with horizontal transfer of ATPase operons. [PDF]
, 2019 Thaumarchaeota are responsible for a significant fraction of ammonia oxidation in the oceans and in soils that range from alkaline to acidic. However, the adaptive mechanisms underpinning their habitat expansion remain poorly understood.
Bartlett, Douglas H +24 more
core +2 more sources