ArticleThe Journal of biological chemistry2009
The tether connecting cytosolic (N terminus) and membrane (C terminus) domains of yeast V-ATPase subunit a (Vph1) is required for assembly of V0 subunit d.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Mechanical inhibition of isolated VeLife · 2020Article
- The 3.5-Å CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase VMolecular cell · 2018Article
- Regulation of Vacuolar H+-ATPase (V-ATPase) Reassembly by Glycolysis Flow in 6-Phosphofructo-1-kinase (PFK-1)-deficient Yeast Cells.The Journal of biological chemistry · 2016Article
- Extra-renal locations of the a4 subunit of H(+)ATPase.BMC cell biology · 2016Article
- Yeast V-ATPase Proteolipid Ring Acts as a Large-conductance Transmembrane Protein Pore.Scientific reports · 2016Article
- Affinity Purification and Structural Features of the Yeast Vacuolar ATPase Vo Membrane Sector.The Journal of biological chemistry · 2015Article
- Yeast phosphofructokinase-1 subunit Pfk2p is necessary for pH homeostasis and glucose-dependent vacuolar ATPase reassembly.The Journal of biological chemistry · 2014Article
- Sorting of the yeast vacuolar-type, proton-translocating ATPase enzyme complex (V-ATPase): identification of a necessary and sufficient Golgi/endosomal retention signal in Stv1p.The Journal of biological chemistry · 2012Article
- Inhibitors of V-ATPase proton transport reveal uncoupling functions of tether linking cytosolic and membrane domains of V0 subunit a (Vph1p).The Journal of biological chemistry · 2012Article
- The reconstructed ancestral subunit a functions as both V-ATPase isoforms Vph1p and Stv1p in Saccharomyces cerevisiae.Molecular biology of the cell · 2011Article
- Inhibition of osteoclast bone resorption by disrupting vacuolar H+-ATPase a3-B2 subunit interaction.The Journal of biological chemistry · 2010Article
- N-terminal domain of the V-ATPase a2-subunit displays integral membrane protein properties.Protein science : a publication of the Protein Society · 2010Article
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Authors and funding
6 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
V-ATPases are molecular motors that reversibly disassemble in vivo. Anchored in the membrane is subunit a. Subunit a has a movable N terminus that switches positions during disassembly and reassembly. Deletions were made at residues securing the N terminus of subunit a (yeast isoform Vph1) to its membrane-bound C-terminal domain in order to understand the role of this conserved region for V-ATPase function. Shrinking of the tether made cells pH-sensitive (vma phenotype) because assembly of V(0) subunit d was harmed. Subunit d did not co-immunoprecipitate with subunit a and the c-ring. Cells contained pools of V(1) and V(0)(-d) that failed to form V(1)V(0), and very low levels of V-ATPase subunits were found at the membrane. Although subunit d expression was stable and at wild-type levels, growth defects were rescued by exogenous VMA6 (subunit d). Stable V(1)V(0) assembled after yeast cells were co-transformed with VMA6 and mutant VPH1. Tether-less V(1)V(0) was delivered to the vacuole and active. It retained 63-71% of the wild-type activity and was responsive to glucose. Tether-less V(1)V(0) disassembled and reassembled after brief glucose depletion and readdition. The N terminus retained binding to V(1) subunits and the C terminus to phosphofructokinase. Thus, no major structural change was generated at the N and C termini of subunit a. We concluded that early steps of V(0) assembly and trafficking were likely impaired by shorter tethers and rescued by VMA6.
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