Structure and Roles of V-type ATPases
T Vasanthakumar, JL Rubinstein - Trends in biochemical sciences, 2020 - cell.com
V-ATPases are membrane-embedded protein complexes that function as ATP hydrolysis-
driven proton pumps. V-ATPases are the primary source of organellar acidification in all …
driven proton pumps. V-ATPases are the primary source of organellar acidification in all …
The H+-ATPase (V-ATPase): from proton pump to signaling complex in health and disease
AF Eaton, M Merkulova… - American Journal of …, 2021 - journals.physiology.org
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 …
gradient across eukaryotic cell membranes, which energizes fundamental cellular …
Molecular basis of V-ATPase inhibition by bafilomycin A1
Pharmacological inhibition of vacuolar-type H+-ATPase (V-ATPase) by its specific inhibitor
can abrogate tumor metastasis, prevent autophagy, and reduce cellular signaling …
can abrogate tumor metastasis, prevent autophagy, and reduce cellular signaling …
Oxidative stress protein Oxr1 promotes V‐ATPase holoenzyme disassembly in catalytic activity‐independent manner
MM Khan, S Lee, S Couoh‐Cardel, RA Oot… - The EMBO …, 2022 - embopress.org
Abstract 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 …
an assembly equilibrium between active holoenzyme and autoinhibited V1‐ATPase and Vo …
RAVE and rabconnectin-3 complexes as signal dependent regulators of organelle acidification
MC Jaskolka, SR Winkley, PM Kane - Frontiers in Cell and …, 2021 - frontiersin.org
The yeast RAVE (Regulator of H+-ATPase of Vacuolar and Endosomal membranes)
complex and Rabconnectin-3 complexes of higher eukaryotes regulate acidification of …
complex and Rabconnectin-3 complexes of higher eukaryotes regulate acidification of …
Coordinated conformational changes in the V1 complex during V-ATPase reversible dissociation
T Vasanthakumar, KA Keon, SA Bueler… - Nature Structural & …, 2022 - nature.com
Abstract Vacuolar-type ATPases (V-ATPases) are rotary enzymes that acidify intracellular
compartments in eukaryotic cells. These multi-subunit complexes consist of a cytoplasmic …
compartments in eukaryotic cells. These multi-subunit complexes consist of a cytoplasmic …
Molecular basis of mEAK7-mediated human V-ATPase regulation
The activity of V-ATPase is well-known to be regulated by reversible dissociation of its V 1
and V o domains in response to growth factor stimulation, nutrient sensing, and cellular …
and V o domains in response to growth factor stimulation, nutrient sensing, and cellular …
Structure of yeast RAVE bound to a partial V1 complex
Vacuolar-type ATPases (V-ATPases) are membrane-embedded proton pumps that acidify
intracellular compartments in almost all eukaryotic cells. Homologous with ATP synthases …
intracellular compartments in almost all eukaryotic cells. Homologous with ATP synthases …
Molecular mechanism of Oxr1p mediated disassembly of yeast V-ATPase
MM Khan, S Wilkens - EMBO reports, 2024 - embopress.org
The eukaryotic vacuolar H+-ATPase (V-ATPase) is regulated by reversible disassembly into
autoinhibited V1-ATPase and Vo proton channel subcomplexes. We recently reported that …
autoinhibited V1-ATPase and Vo proton channel subcomplexes. We recently reported that …
Tender love and disassembly: How a TLDc domain protein breaks the V‐ATPase
S Wilkens, MM Khan, K Knight, RA Oot - Bioessays, 2023 - Wiley Online Library
Abstract Vacuolar ATPases (V‐ATPases, V1Vo‐ATPases) are rotary motor proton pumps
that acidify intracellular compartments, and, when localized to the plasma membrane, the …
that acidify intracellular compartments, and, when localized to the plasma membrane, the …