Regulation of proton-translocating V-ATPases [PDF]
Journal of Experimental Biology, 1997 ABSTRACT Vacuolar-type ATPases (V-ATPases) are proton-translocating enzymes that occur in the endomembranes of all eukaryotes and in the plasma membranes of many eukaryotes. They are multisubunit, heteromeric proteins composed of two structural domains, a peripheral, catalytic V1 domain and a membrane-spanning Vo domain.
H, Merzendorfer +4 more
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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
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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
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
The V-ATPase complex component RNAseK is required for lysosomal hydrolase delivery and autophagosome degradation. [PDF]
Nat CommunMakar AN +10 more
europepmc +3 more sources
A cell-based assay for CD63-containing extracellular vesicles [PDF]
, 2019 Extracellular vesicles (EVs) are thought to be important in cell-cell communication and have elicited extraordinary interest as potential biomarkers of disease. However, quantitative methods to enable elucidation of mechanisms underlying release are few.
Cashikar, Anil G, Hanson, Phyllis I
core +2 more sources
Regulation of V-ATPase activity
Frontiers in Bioscience, 2017 V-ATPases are ATP-driven proton pumps present in both intracellular and cell surface membranes of eukaryotes that function in many normal and disease processes. V-ATPases are large, multi-subunit complexes composed of a peripheral domain (V1) that hydrolyzes ATP and a membrane integral domain (V0) that translocates protons.
Christina, McGuire +3 more
openaire +2 more sources
Retrieval of the vacuolar H-ATPase from phagosomes revealed by live cell imaging. [PDF]
PLoS ONE, 2010 BackgroundThe vacuolar H+-ATPase, or V-ATPase, is a highly-conserved multi-subunit enzyme that transports protons across membranes at the expense of ATP.
Margaret Clarke +3 more
doaj +1 more source
Saccharomyces cerevisiae mutants affected in vacuole assembly or vacuolar H+-ATPase are hypersensitive to lead (Pb) toxicity [PDF]
, 2014 Lead is an important environmental pollutant. The role of vacuole, in Pb detoxification, was studied using a vacuolar protein sorting mutant strain (vps16Δ), belonging to class C mutants.
A Richards +34 more
core +1 more source
F-actin reorganization by V-ATPase inhibition in prostate cancer
Biology Open, 2017 The vacuolar ATPase (V-ATPase) proton pump sustains cellular pH homeostasis, and its inhibition triggers numerous stress responses. However, the cellular mechanisms involved remain largely elusive in cancer cells.
Yamhilette Licon-Munoz +3 more
doaj +1 more source