ArticleMolecular biology of the cell2008
Voa1p functions in V-ATPase assembly in the yeast endoplasmic reticulum.
Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 52 citations in OpenAlex.
- The Lack of a COPII Cargo Receptor Erv14 Impacts Physiological Functions of the Vacuole in Saccharomyces cerevisiae.Traffic (Copenhagen, Denmark) · 2026Article
- Recent advances in the clinical spectrum and pathomechanisms associated with X-linked myopathy with excessive autophagy and otherJournal of neuromuscular diseases · 2025Review
- Targeting vacuolar ATPase in tobacco whitefly,Journal of biosciences · 2025Review
- Big1 is a newly identified autophagy regulator that is critical for a fully functional V-ATPase.Molecular biology of the cell · 2024Article
- Genome-Scale Screening ofJournal of fungi (Basel, Switzerland) · 2024Article
- Tender love and disassembly: How a TLDc domain protein breaks the V-ATPase.BioEssays : news and reviews in molecular, cellular and developmental biology · 2023Article
- Structural basis of V-ATPase VProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Mutations in V-ATPase in follicular lymphoma activate autophagic flux creating a targetable dependency.Autophagy · 2023Article
- Follicular lymphoma-associated mutations in the V-ATPase chaperone VMA21 activate autophagy creating a targetable dependency.Autophagy · 2022Article
- Follicular lymphoma-associated mutations in the V-ATPase chaperone Vma21 activate autophagy by dysfunctional V-ATPase assembly.Autophagy reports · 2022Article
- The Plant V-ATPase.Frontiers in plant science · 2022Review
- Mutations in the V-ATPase Assembly Factor VMA21 Cause a Congenital Disorder of Glycosylation With Autophagic Liver Disease.Hepatology (Baltimore, Md.) · 2020Article
- Regulation and function of V-ATPases in physiology and disease.Biochimica et biophysica acta. Biomembranes · 2020Review
- Structures of a Complete Human V-ATPase Reveal Mechanisms of Its Assembly.Molecular cell · 2020Article
- Structure of V-ATPase from the mammalian brain.Science (New York, N.Y.) · 2020Article
- Article
- ATP6AP2 functions as a V-ATPase assembly factor in the endoplasmic reticulum.Molecular biology of the cell · 2018Article
- Some assembly required: Contributions of Tom Stevens' lab to the V-ATPase field.Traffic (Copenhagen, Denmark) · 2018Review
- The 3.5-Å CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase VMolecular cell · 2018Article
- Molecular mechanisms of cutis laxa- and distal renal tubular acidosis-causing mutations in V-ATPaseThe Journal of biological chemistry · 2018Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The yeast Saccharomyces cerevisiae vacuolar ATPase (V-ATPase) is a multisubunit complex divided into two sectors: the V(1) sector catalyzes ATP hydrolysis and the V(0) sector translocates protons, resulting in acidification of its resident organelle. Four protein factors participate in V(0) assembly. We have discovered a fifth V(0) assembly factor, Voa1p (YGR106C); an endoplasmic reticulum (ER)-localized integral membrane glycoprotein. The role of Voa1p in V(0) assembly was revealed in cells expressing an ER retrieval-deficient form of the V-ATPase assembly factor Vma21p (Vma21pQQ). Loss of Voa1p in vma21QQ yeast cells resulted in loss of V-ATPase function; cells were unable to acidify their vacuoles and exhibited growth defects typical of cells lacking V-ATPase. V(0) assembly was severely compromised in voa1 vma21QQ double mutants. Isolation of V(0)-Vma21p complexes indicated that Voa1p associates most strongly with Vma21p and the core proteolipid ring of V(0) subunits c, c', and c''. On assembly of the remaining three V(0) subunits (a, d, and e) into the V(0) complex, Voa1p dissociates from the now fully assembled V(0)-Vma21p complex. Our results suggest Voa1p functions with Vma21p early in V(0) assembly in the ER, but then it dissociates before exit of the V(0)-Vma21p complex from the ER for transport to the Golgi compartment.
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