V-type Atpase
V-type Atpase - Related Videos
07:38
Measuring In Vitro ATPase Activity for Enzymatic Characterization
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Cited by 27 •
2016
We describe a basic protocol for quantitating in vitro ATPase activity. This protocol can be optimized based on the level of activity and requirements for a given purified ATPase.
08:44
Isolation of F1-ATPase from the Parasitic Protist Trypanosoma brucei
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Cited by 1 •
2019
This protocol describes the purification of F1-ATPase from the cultured insect stage of Trypanosoma brucei. The procedure yields a highly pure, homogeneous, and active complex suitable for structural and enzymatic studies.
12:07
Chemical Modification of the Tryptophan Residue in a Recombinant Ca2+-ATPase N-domain for Studying Tryptophan-ANS FRET
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2021
ANS binds to the Ca2+-ATPase recombinant N-domain. Fluorescence spectra display a FRET-like pattern upon excitation at a wavelength of 295 nm. NBS-mediated chemical modification of Trp quenches the fluorescence of the N-domain, which leads to the absence of energy transfer (FRET) between the Trp residue and ANS.
08:37
Purification of the Sarco-Endoplasmic Reticulum Ca2+-ATPase from Rabbit Muscle
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2025
This protocol describes an improved SERCA purification method, which includes the disaccharide trehalose in the final centrifugation step. This carbohydrate stabilizes proteins under harsh conditions. The purified SERCA was catalytically active and displayed high purity, making it suitable for structural and functional studies.
10:07
Isolation of Type I and Type II Pericytes from Mouse Skeletal Muscles
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Cited by 11 •
2017
This work describes a FACS-based protocol that allows for easy and simultaneous isolation of type I and type II pericytes from skeletal muscles.
FAQs
Energy conversion depends on mechanical coupling between its two sectors. ATP hydrolysis in the cytosolic V1 sector drives rotational movement, and that rotation powers the membrane-embedded Vo sector. This arrangement links a chemical reaction, ATP breakdown, to directional proton translocation, allowing the complex to regulate membrane acidity rather than merely consume ATP.
Rotational movement provides the physical connection between energy release and transport. As the V1 sector hydrolyzes ATP, its resulting motion is transmitted to the Vo sector, which uses that mechanical input to move protons across the membrane. Without this coupling, ATP hydrolysis and proton translocation would not operate as one coordinated process.
Proton transport establishes acidity within selected cellular compartments. That acidity helps cells control conditions in lysosomes, endosomes, secretory vesicles, and other organelles, where local chemical environments support degradation, membrane trafficking, and ion regulation. Thus, V-ATPase activity connects membrane transport with the functional organization of intracellular compartments.
Lysosomes, endosomes, and secretory vesicles are among the compartments whose acidity is controlled by V-ATPase activity. The resulting proton gradient contributes to their specialized functions, including protein degradation and membrane trafficking. Studying the enzyme in these locations helps explain how cells maintain distinct internal environments within different membrane-bound organelles.
By acidifying lysosomes and endosomes, V-ATPase helps create the compartment conditions associated with protein degradation and membrane trafficking. Its activity therefore affects more than proton concentration alone: it supports the operation of cellular pathways that process material and move membranes or cargo between intracellular locations.
V-ATPase contributes to specialized processes such as bone resorption, extending its importance beyond general organelle acidification. Its role in this physiological process, together with connections to cellular physiology and disease mechanisms, makes the complex a subject of therapeutic-targeting research. Investigators can therefore examine it both as a biological regulator and as a possible intervention point.