ArticleProceedings of the National Academy of Sciences of the United States of America2007
Excess vacuolar SNAREs drive lysis and Rab bypass fusion.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 81 citations in OpenAlex.
- Functional assembly of the Qc-SNARE with Sec18 and Sec17 on membranes.Molecular biology of the cell · 2026Article
- Differential effects of lysophospholipid headgroups, acyl chain length and saturation on vacuole acidification, CaFrontiers in cell and developmental biology · 2026Article
- The Hidden Cost of Fusion: Intrinsic Asymmetry in Vesicle Fusion Restricts Synthetic Cell Growth.bioRxiv : the preprint server for biology · 2025Article
- Yeast lunapark regulates the formation ofiScience · 2023Article
- Human atlastins are sufficient to drive the fusion of liposomes with a physiological lipid composition.The Journal of cell biology · 2023Article
- A Genome-Wide Screen Reveals That Endocytic Genes Are Important for Pma1p Asymmetry during Cell Division inInternational journal of molecular sciences · 2022Article
- Phosphatidylinositol 3,5-bisphosphate regulates CaTraffic (Copenhagen, Denmark) · 2020Article
- Continuum Models of Membrane Fusion: Evolution of the Theory.International journal of molecular sciences · 2020Review
- Copper blocks V-ATPase activity and SNARE complex formation to inhibit yeast vacuole fusion.Traffic (Copenhagen, Denmark) · 2019Article
- Phosphatidylinositol 3,5-bisphosphate regulates the transition between trans-SNARE complex formation and vacuole membrane fusion.Molecular biology of the cell · 2019Article
- Highly Efficient Protein-free Membrane Fusion: A Giant Vesicle Study.Biophysical journal · 2019Article
- Deleting the DAG kinase Dgk1 augments yeast vacuole fusion through increased Ypt7 activity and altered membrane fluidity.Traffic (Copenhagen, Denmark) · 2017Article
- A cascade of multiple proteins and lipids catalyzes membrane fusion.Molecular biology of the cell · 2017Review
- Improved reconstitution of yeast vacuole fusion with physiological SNARE concentrations reveals an asymmetric Rab(GTP) requirement.Molecular biology of the cell · 2016Article
- High Transmembrane Voltage Raised by Close Contact Initiates Fusion Pore.Frontiers in molecular neuroscience · 2016Article
- Exocytotic fusion pores are composed of both lipids and proteins.Nature structural & molecular biology · 2016Article
- A LAPF/phafin1-like protein regulates TORC1 and lysosomal membrane permeabilization in response to endoplasmic reticulum membrane stress.Molecular biology of the cell · 2015Article
- Identification of siRNA delivery enhancers by a chemical library screen.Nucleic acids research · 2015Article
- SNAREs support atlastin-mediated homotypic ER fusion in Saccharomyces cerevisiae.The Journal of cell biology · 2015Article
- Abscisic acid prevents the coalescence of protein storage vacuoles by upregulating expression of a tonoplast intrinsic protein gene in barley aleurone.Journal of experimental botany · 2015Article
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3 authors at 2 institutions in 1 country.
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Abstract
Although concentrated soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) drive liposome fusion and lysis, the fusion of intracellular membranes also requires Rab GTPases, Rab effectors, SM proteins, and specific regulatory lipids and is accompanied by little or no lysis. To rationalize these findings, we generated yeast strains that overexpress all four vacuolar SNAREs (4SNARE(++)). Although vacuoles with physiological levels of Rab, Rab effector/SM complex, and SNAREs support rapid fusion without Rab- and SNARE-dependent lysis, vacuoles from 4SNARE(++) strains show extensive lysis and a reduced need for the Rab Ypt7p or regulatory lipids for fusion. SNARE overexpression and the addition of pure homotypic fusion and vacuole protein sorting complex (HOPS), which bears the vacuolar SM protein, enables ypt7Delta vacuoles to fuse, allowing direct comparison of Rab-dependent and Rab-independent fusion. Because 3- to 40-fold more of each of the five components that form the SNARE/HOPS fusion complex are required for vacuoles from ypt7Delta strains to fuse at the same rate as vacuoles from wild-type strains, the apparent forward rate constant of 4SNARE/HOPS complex assembly is enhanced many thousand-fold by Ypt7p. Rabs function in normal membrane fusion by concentrating SNAREs, other proteins (e.g., SM), and key lipids at a fusion site and activating them for fusion without lysis.
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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.