ArticleThe Journal of biological chemistry2012
Subunit interactions at the V1-Vo interface in yeast vacuolar ATPase.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 46 citations in OpenAlex.
- Human V-ATPase function is positively and negatively regulated by TLDc proteins.Structure (London, England : 1993) · 2024Article
- Human V-ATPase a-subunit isoforms bind specifically to distinct phosphoinositide phospholipids.The Journal of biological chemistry · 2023Article
- Tender love and disassembly: How a TLDc domain protein breaks the V-ATPase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Chimeric a-subunit isoforms generate functional yeast V-ATPases with altered regulatory properties in vitro and in vivo.Molecular biology of the cell · 2023Article
- The cytosolic N-terminal domain of V-ATPase a-subunits is a regulatory hub targeted by multiple signals.Frontiers in molecular biosciences · 2023Review
- Regulation and function of V-ATPases in physiology and disease.Biochimica et biophysica acta. Biomembranes · 2020Review
- Mechanical inhibition of isolated VeLife · 2020Article
- Functional reconstitution of vacuolar HThe Journal of biological chemistry · 2019Article
- MgATP hydrolysis destabilizes the interaction between subunit H and yeast VThe Journal of biological chemistry · 2018Article
- Clathrin coat controls synaptic vesicle acidification by blocking vacuolar ATPase activity.eLife · 2018Article
- The Peripheral Stalk of Rotary ATPases.Frontiers in physiology · 2018Review
- Direct interaction of the Golgi V-ATPase a-subunit isoform with PI(4)P drives localization of Golgi V-ATPases in yeast.Molecular biology of the cell · 2017Article
- Chemical screening identifies ATM as a target for alleviating senescence.Nature chemical biology · 2017Article
- Breaking up and making up: The secret life of the vacuolar HProtein science : a publication of the Protein Society · 2017Review
- Biolayer interferometry of lipid nanodisc-reconstituted yeast vacuolar HProtein science : a publication of the Protein Society · 2017Article
- Crystal structure of yeast V1-ATPase in the autoinhibited state.The EMBO journal · 2016Article
- Regulation of V-ATPase assembly and function of V-ATPases in tumor cell invasiveness.Biochimica et biophysica acta · 2016Review
- Organelle acidification negatively regulates vacuole membrane fusion in vivo.Scientific reports · 2016Article
- Proton Transport and pH Control in Fungi.Advances in experimental medicine and biology · 2016Review
- Affinity Purification and Structural Features of the Yeast Vacuolar ATPase Vo Membrane Sector.The Journal of biological chemistry · 2015Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Eukaryotic vacuolar ATPase (V-ATPase) is regulated by a reversible dissociation mechanism that involves breaking and reforming of protein-protein interactions at the interface of the V(1)-ATPase and V(o)-proton channel domains. We found previously that the head domain of the single copy C subunit (C(head)) binds one subunit EG heterodimer with high affinity (Oot, R.A. and Wilkens, S. (2010) J. Biol. Chem. 285, 24654-24664). Here we generated a water-soluble construct of the N-terminal domain of the V(o) "a" subunit composed of amino acid residues 104-372 (a(NT(104-372))). Analytical gel filtration chromatography and sedimentation velocity analysis revealed that a(NT(104-372)) undergoes reversible dimerization in a concentration-dependent manner. A low-resolution molecular envelope was calculated for the a(NT(104-372)) dimer using small angle x-ray scattering data. Isothermal titration calorimetry experiments revealed that a(NT(104-372)) binds the C(foot) and EG heterodimer with dissociation constants of 22 and 33 μM, respectively. We speculate that the spatial closeness of the a(NT), C(foot), and EG binding sites in the intact V-ATPase results in a high-avidity interaction that is able to resist the torque of rotational catalysis, and that reversible enzyme dissociation is initiated by breaking either the a(NT(104-372))-C(foot) or a(NT(104-372))-EG interaction by an as-yet unknown signaling mechanism.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.