Cryo-EM structures of intact V-ATPase from bovine brain
Nature Communications, 2020 The vacuolar-type H+ -ATPases (V-ATPase) hydrolyze ATP to pump protons across the plasma or intracellular membrane. Here authors report two cryo-EM structures of the intact V-ATPase from bovine brain with all the subunits including the subunit H, which ...
Rong Wang +6 more
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V-ATPase C Acts as a Receptor for Bacillus thuringiensis Cry2Ab and Enhances Cry2Ab Toxicity to Helicoverpa armigera [PDF]
InsectsCry2Ab is a significant alternative Bacillus thuringiensis (Bt) protein utilized for managing insect resistance to Cry1 toxins and broadening the insecticidal spectrum of crops containing two or more Bt genes. Unfortunately, the identified receptors fail
Pin Li +7 more
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TBC1D24 interacts with the v-ATPase and regulates intraorganellar pH in neurons [PDF]
iScienceSummary: The vacuolar ATPase (v-ATPase) is essential for acidification of intracellular organelles, including synaptic vesicles. Its activity is controlled by cycles of association and dissociation of the ATP hydrolysis (V1) and proton transport (V0 ...
Sara Pepe +10 more
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Luminal Acidification of Diverse Organelles by V-ATPase in Animal Cells [PDF]
, 2000 Eukaryotic cells contain organelles bounded by a single membrane in the cytoplasm. These organelles have differentiated to carry out various functions in the pathways of endocytosis and exocytosis. Their lumina are acidic, with pH ranging from 4.5 to 6.5.
Masamitsu Futai +5 more
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Structure of V-ATPase from the mammalian brain
Science, 2020 Snapshots of a rotary pump Vesicular- or vacuolar-type adenosine triphosphatases (V-ATPases) are ATP-hydrolysis–driven proton pumps. In neurons, V-ATPase activity generates a proton gradient across the membrane of synaptic vesicles so that ...
Y. M. Abbas +4 more
semanticscholar +6 more sources
The yeast protein kinase Sch9 adjusts V-ATPase assembly/disassembly to control pH homeostasis and longevity in response to glucose availability. [PDF]
PLoS Genetics, 2017 The conserved protein kinase Sch9 is a central player in the nutrient-induced signaling network in yeast, although only few of its direct substrates are known.
Tobias Wilms +12 more
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Molecular basis for the binding and modulation of V-ATPase by a bacterial effector protein. [PDF]
PLoS Pathogens, 2017 Intracellular pathogenic bacteria evade the immune response by replicating within host cells. Legionella pneumophila, the causative agent of Legionnaires' Disease, makes use of numerous effector proteins to construct a niche supportive of its replication
Jianhua Zhao +11 more
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Regulation of V-ATPase Assembly in Nutrient Sensing and Function of V-ATPases in Breast Cancer Metastasis [PDF]
Frontiers in Physiology, 2018 V-ATPases are proton pumps that function to acidify intracellular compartments in all eukaryotic cells, and to transport protons across the plasma membrane of certain specialized cells.
Michaela Collins, M. Forgac
semanticscholar +4 more sources
ADP Inhibition of Myosin V ATPase Activity [PDF]
Biophysical Journal, 2000 The kinetic mechanism of myosin V is of great interest because recent evidence indicates that the two-headed myosin V molecule functions as a processive motor, i.e., myosin V is capable of moving along an actin filament for many catalytic cycles of the motor without dissociating.
Enrique M. De La Cruz +2 more
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Disease Models & Mechanisms, 2021 The vacuolar-type H+-ATPase (V-ATPase) is a multi-subunit proton pump that regulates cellular pH. V-ATPase activity modulates several cellular processes, but cell-type-specific functions remain poorly understood.
Peu Santra, Jeffrey D. Amack
doaj +1 more source