ArticleThe Journal of biological chemistry2009
Complex lipid requirements for SNARE- and SNARE chaperone-dependent membrane fusion.
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 39 papers.
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Who cites it
39 citing papers in PubMed, 72 citations in OpenAlex.
- Lipidomic signatures associated with cognitive impairment in type 1 diabetes mellitus: a pilot study integrating clinical serum and mouse hippocampus.Journal of translational medicine · 2026Article
- Who's in control? Principles of Rab GTPase activation in endolysosomal membrane trafficking and beyond.The Journal of cell biology · 2021Review
- Phosphatidylinositol 3,5-bisphosphate regulates CaTraffic (Copenhagen, Denmark) · 2020Article
- Synergistic lipid compositions for albumin receptor mediated delivery of mRNA to the liver.Nature communications · 2020Article
- 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
- 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
- Phosphatidic Acid: From Pleiotropic Functions to Neuronal Pathology.Frontiers in cellular neuroscience · 2019Review
- Regulation of Membrane Turnover by Phosphatidic Acid: Cellular Functions and Disease Implications.Frontiers in cell and developmental biology · 2019Review
- Determination of Sec18-Lipid Interactions by Liposome-Binding Assay.Methods in molecular biology (Clifton, N.J.) · 2019Article
- Molecular basis of selective mitochondrial fusion by heterotypic action between OPA1 and cardiolipin.Nature cell biology · 2017Article
- The Multifaceted Role of SNARE Proteins in Membrane Fusion.Frontiers in physiology · 2017Review
- Phosphatidylinositol (3,4,5)-trisphosphate binds to sortilin and competes with neurotensin: Implications for very low density lipoprotein binding.Biochemical and biophysical research communications · 2016Article
- Phosphatidic Acid Sequesters Sec18p from cis-SNARE Complexes to Inhibit Priming.Traffic (Copenhagen, Denmark) · 2016Article
- The Central Polybasic Region of the Soluble SNARE (Soluble N-Ethylmaleimide-sensitive Factor Attachment Protein Receptor) Vam7 Affects Binding to Phosphatidylinositol 3-Phosphate by the PX (Phox Homology) Domain.The Journal of biological chemistry · 2016Article
- Physiological lipid composition is vital for homotypic ER membrane fusion mediated by the dynamin-related GTPase Sey1p.Scientific reports · 2016Article
- Phospholipase C and D regulation of Src, calcium release and membrane fusion during Xenopus laevis development.Developmental biology · 2015Review
- Lipid molecules influence early stages of yeast SNARE-mediated membrane fusion.Physical biology · 2015Article
- The Habc domain of the SNARE Vam3 interacts with the HOPS tethering complex to facilitate vacuole fusion.The Journal of biological chemistry · 2015Article
- Diacylglycerol, phosphatidic acid, and their metabolic enzymes in synaptic vesicle recycling.Advances in biological regulation · 2015Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Membrane fusion without lysis has been reconstituted with purified yeast vacuolar SNAREs (soluble N-ethylmaleimide-sensitive factor attachment protein receptors), the SNARE chaperones Sec17p/Sec18p and the multifunctional HOPS complex, which includes a subunit of the SNARE-interactive Sec1-Munc18 family, and vacuolar lipids: phosphatidylcholine (PC), phosphatidylethanolamine (PE), phosphatidylinositol (PI), phosphatidylserine (PS), phosphatidic acid (PA), cardiolipin (CL), ergosterol (ERG), diacylglycerol (DAG), and phosphatidylinositol 3-phosphate (PI3P). We now report that many of these lipids are required for rapid and efficient fusion of the reconstituted SNARE proteoliposomes in the presence of SNARE chaperones. Omission of either PE, PA, or PI3P from the complete set of lipids strongly reduces fusion, and PC, PE, PA, and PI3P constitute a minimal set of lipids for fusion. PA could neither be replaced by other lipids with small headgroups such as DAG or ERG nor by the acidic lipids PS or PI. PA is needed for full association of HOPS and Sec18p with proteoliposomes having a minimal set of lipids. Strikingly, PA and PE are as essential for SNARE complex assembly as for fusion, suggesting that these lipids facilitate functional interactions among SNAREs and SNARE chaperones.
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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.