Results 71 to 80 of about 9,362,172 (272)

A thermo-physical analysis of the proton pump vacuolar-ATPase: the constructal approach [PDF]

open access: yes, 2014
Pumping protons across a membrane was a critical step at the origin of life on earth, and it is still performed in all living organisms, including in human cells. Proton pumping is paramount to keep normal cells alive, e.g.
Deisboeck, Thomas S.   +2 more
core   +2 more sources

Plasma membrane v-ATPase controls oncogenic Ras-induced macropinocytosis

open access: yesNature, 2019
Oncogenic activation of RAS is associated with the acquisition of a unique set of metabolic dependencies that contribute to tumour cell fitness. Cells that express oncogenic RAS are able to internalize and degrade extracellular protein via a fluid-phase ...
Craig Ramirez   +3 more
semanticscholar   +1 more source

AMPK:Sensing Glucose as well as Cellular Energy Status [PDF]

open access: yes, 2018
Mammalian AMPK is known to be activated by falling cellular energy status, signaled by rising AMP/ATP and ADP/ATP ratios. We review recent information about how this occurs but also discuss new studies suggesting that AMPK is able to sense glucose ...
Hardie, David, Lin, Sheng-Cai
core   +2 more sources

Rotation of the Proteolipid Ring in the V-ATPase [PDF]

open access: yesJournal of Biological Chemistry, 2003
V0V1-ATPase is a proton-translocating ATPase responsible for acidification of eukaryotic intracellular compartments and for ATP synthesis in archaea and some eubacteria. We demonstrated recently the rotation of the central stalk subunits in V1, a catalytic sector of V0V1-ATPase (Imamura, H., Nakano, M., Noji, H., Muneyuki, E., Ohkuma, S., Yoshida, M ...
Yokoyama   +4 more
openaire   +3 more sources

RAVE and Rabconnectin-3 Complexes as Signal Dependent Regulators of Organelle Acidification

open access: yesFrontiers in Cell and Developmental Biology, 2021
The yeast RAVE (Regulator of H+-ATPase of Vacuolar and Endosomal membranes) complex and Rabconnectin-3 complexes of higher eukaryotes regulate acidification of organelles such as lysosomes and endosomes by catalyzing V-ATPase assembly.
Michael C. Jaskolka   +2 more
doaj   +1 more source

Infrared spectroscopic studies on the V-ATPase

open access: yesBiochimica et Biophysica Acta (BBA) - Bioenergetics, 2015
V-ATPase is an ATP-driven rotary motor that vectorially transports ions. Together with F-ATPase, a homologous protein, several models on the ion transport have been proposed, but their molecular mechanisms are yet unknown. V-ATPase from Enterococcus hirae forms a large supramolecular protein complex (total molecular weight: ~700,000) and ...
Hideki Kandori   +2 more
openaire   +3 more sources

Transient Receptor Potential V Channels Are Essential for Glucose Sensing by Aldolase and AMPK [PDF]

open access: yes, 2019
Fructose-1,6-bisphosphate (FBP) aldolase links sensing of declining glucose availability to AMPK activation via the lysosomal pathway. However, how aldolase transmits lack of occupancy by FBP to AMPK activation remains unclear.
Changchuan Xie   +34 more
core   +5 more sources

Specific V-ATPase expression sub-classifies IDHwt lower-grade gliomas and impacts glioma growth in vivoResearch in context

open access: yesEBioMedicine, 2019
Background: Cancer cells use specific V-ATPase subunits to activate oncogenic pathways. Therefore, we investigated V-ATPase deregulation in aggressive gliomas and associated signaling.
Andrea Terrasi   +11 more
doaj   +1 more source

AKT Ser/Thr kinase increases V-ATPase–dependent lysosomal acidification in response to amino acid starvation in mammalian cells

open access: yesJournal of Biological Chemistry, 2020
The vacuolar H+-ATPase (V-ATPase) is an ATP-dependent proton pump that is essential for cellular homeostasis. V-ATPase activity is controlled by the regulated assembly of the enzyme from its component V1 and V0 domains.
Michael Patrick Collins   +2 more
semanticscholar   +1 more source

Regulation of V‐ATPases by reversible disassembly [PDF]

open access: yesFEBS Letters, 2000
V‐ATPases consist of a complex of peripheral subunits containing catalytic sites for ATP hydrolysis, the V1 sector, attached to several membrane subunits containing a proton pore, the V0 sector. ATP‐driven proton transport requires structural and functional coupling of the two sectors, but in vivo, the interaction between the V1 and V0 sectors is ...
openaire   +3 more sources

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