ArticleBiophysical journal2003
Diacylglycerol-rich domain formation in giant stearoyl-oleoyl phosphatidylcholine vesicles driven by phospholipase C activity.
Article in Biophysical journal, 2003. 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, 31 citations in OpenAlex.
- Acute diacylglycerol production activates critical membrane-shaping proteins leading to mitochondrial tubulation and fission.Nature communications · 2025Article
- Mechanism of two styryl BODIPYs as fluorescent probes and protective agents in lipid bilayers against aqueous ClORSC advances · 2024Article
- Roles for diacylglycerol in synaptic vesicle priming and release revealed by complete reconstitution of core protein machinery.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Novel Roles for Diacylglycerol in Synaptic Vesicle Priming and Release Revealed by Complete Reconstitution of Core Protein Machinery.bioRxiv : the preprint server for biology · 2023Article
- Review
- pH-Tolerant giant vesicles composed of cationic lipids with imine linkages and oleic acids.RSC advances · 2020Article
- Excess diacylglycerol at the endoplasmic reticulum disrupts endomembrane homeostasis and autophagy.BMC biology · 2020Article
- End-product diacylglycerol enhances the activity of PI-PLC through changes in membrane domain structure.Biophysical journal · 2015Article
- Phospholipases may play multiple roles in anisotropic plant cell growth.Protoplasma · 2013Article
- A simple method for the reconstitution of membrane proteins into giant unilamellar vesicles.The Journal of membrane biology · 2010Article
- A common mechanism underlies stretch activation and receptor activation of TRPC6 channels.Proceedings of the National Academy of Sciences of the United States of America · 2006Article
- Asymmetric addition of ceramides but not dihydroceramides promotes transbilayer (flip-flop) lipid motion in membranes.Biophysical journal · 2005Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
We have studied the effect of phospholipase C from Bacillus cereus and Clostridium perfringens (alpha-toxin) on giant stearoyl-oleoyl phosphatidylcholine (SOPC) vesicles. Enzyme activity leads to a binary mixture of SOPC and the diacylglycerol SOG, which phase separates into a SOPC-rich bilayer phase and a SOG-rich isotropic bulk-like domain embedded within the membrane, as seen directly by phase contrast microscopy. After prolonged enzymatic attack, all bilayer membranes are transformed into an isotropic pure SOG phase as characterized by fluorescence microscopy, differential scanning calorimetry, fluorescence anisotropy measurements, and small angle x-ray scattering. These domains may have biological relevance, serving as storage compartments for hydrophobic molecules and/or catalyzing cellular signaling events at their boundaries. Furthermore, in the early stages of asymmetric enzymatic attack to the external monolayer of giant vesicles, we observe a transient coupling of the second-messenger diacylglycerol to membrane spontaneous curvature, which decreases due to enzyme activity, before domain formation and final vesicle collapse occurs.
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