ArticleTraffic (Copenhagen, Denmark)2016
Phosphatidic Acid Sequesters Sec18p from cis-SNARE Complexes to Inhibit Priming.
Article in Traffic (Copenhagen, Denmark), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
20 citing papers in PubMed, 40 citations in OpenAlex.
- Functional assembly of the Qc-SNARE with Sec18 and Sec17 on membranes.Molecular biology of the cell · 2026Article
- Article
- Use of Bio-Layer Interferometry (BLI) to Measure Binding Affinities of SNAREs and Phosphoinositides.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Spectroscopic Methods for Detecting Conformational Changes During Sec18-Lipid Interactions.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Phosphatidic acid signaling and function in nuclei.Progress in lipid research · 2024Review
- Phospholipase Dδ and phosphatidic acid mediate heat-induced nuclear localization of glyceraldehyde-3-phosphate dehydrogenase in Arabidopsis.The Plant journal : for cell and molecular biology · 2022Article
- New Era of Diacylglycerol Kinase, Phosphatidic Acid and Phosphatidic Acid-Binding Protein.International journal of molecular sciences · 2020Review
- Phosphatidylinositol 3,5-bisphosphate regulates CaTraffic (Copenhagen, Denmark) · 2020Article
- Interplay Between SNX27 and DAG Metabolism in the Control of Trafficking and Signaling at the IS.International journal of molecular sciences · 2020Review
- A small-molecule competitive inhibitor of phosphatidic acid binding by the AAA+ protein NSF/Sec18 blocks the SNARE-priming stage of vacuole fusion.The Journal of biological chemistry · 2019Article
- Copper blocks V-ATPase activity and SNARE complex formation to inhibit yeast vacuole fusion.Traffic (Copenhagen, Denmark) · 2019Article
- The inner workings of intracellular heterotypic and homotypic membrane fusion mechanisms.Journal of biosciences · 2019Article
- The Participation of Regulatory Lipids in Vacuole Homotypic Fusion.Trends in biochemical sciences · 2019Review
- Phosphatidic acid induces conformational changes in Sec18 protomers that prevent SNARE priming.The Journal of biological chemistry · 2019Article
- Phosphatidylinositol 3,5-bisphosphate regulates the transition between trans-SNARE complex formation and vacuole membrane fusion.Molecular biology of the cell · 2019Article
- Determination of Sec18-Lipid Interactions by Liposome-Binding Assay.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Use of Surface Plasmon Resonance (SPR) to Determine Binding Affinities and Kinetic Parameters Between Components Important in Fusion Machinery.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Use of Microscale Thermophoresis (MST) to Measure Binding Affinities of Components of the Fusion Machinery.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Host phosphatidic acid phosphatase lipin1 is rate limiting for functional hepatitis C virus replicase complex formation.PLoS pathogens · 2018Article
- Deleting the DAG kinase Dgk1 augments yeast vacuole fusion through increased Ypt7 activity and altered membrane fluidity.Traffic (Copenhagen, Denmark) · 2017Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Yeast vacuole fusion requires the activation of cis-SNARE complexes through priming carried out by Sec18p/N-ethylmaleimide sensitive factor and Sec17p/α-SNAP. The association of Sec18p with vacuolar cis-SNAREs is regulated in part by phosphatidic acid (PA) phosphatase production of diacylglycerol (DAG). Inhibition of PA phosphatase activity blocks the transfer of membrane-associated Sec18p to SNAREs. Thus, we hypothesized that Sec18p associates with PA-rich membrane microdomains before transferring to cis-SNARE complexes upon PA phosphatase activity. Here, we examined the direct binding of Sec18p to liposomes containing PA or DAG. We found that Sec18p preferentially bound to liposomes containing PA compared with those containing DAG by approximately fivefold. Additionally, using a specific PA-binding domain blocked Sec18p binding to PA-liposomes and displaced endogenous Sec18p from isolated vacuoles. Moreover, the direct addition of excess PA blocked the priming activity of isolated vacuoles in a manner similar to chemically inhibiting PA phosphatase activity. These data suggest that the conversion of PA to DAG facilitates the recruitment of Sec18p to cis-SNAREs. Purified vacuoles from yeast lacking the PA phosphatase Pah1p showed reduced Sec18p association with cis-SNAREs and complementation with plasmid-encoded PAH1 or recombinant Pah1p restored the interaction. Taken together, this demonstrates that regulating PA concentrations by Pah1p activity controls SNARE priming by Sec18p.
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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.