title: Lipid sorting by ceramide and the consequences for membrane proteins.
abstract: We mimicked the effect of sphingomyelinase activity on lipid mixtures of palmitoyl-oleoyl-phosphatidylcholine, sphingomyelin, ceramide, and 10 mol % cholesterol. Using x-ray diffraction experiments in combination with osmotic stress we found, in agreement with previous studies, that ceramide induces a coexistence of L(α) and L(β) domains. A detailed structural analysis of the coexisting domains demonstrated an increase of lipid packing density and membrane thickness in the L(α) domains upon increasing overall ceramide levels. This provides evidence for a ceramide-driven accumulation of cholesterol in the L(α) domains, in support of previous reports. We further determined the bending rigidities of the coexisting domains and found that the accumulation of cholesterol in the L(α) domains stabilizes their bending rigidity, which experiences a dramatic drop in the absence of cholesterol. Deriving experimental estimates for the spontaneous curvature and Gaussian modulus of curvature, we show, using a simple geometric model for ion channels, that in this way changes in the conformational equilibrium of membrane proteins can be kept small.
authors: Institute of Biophysics and Nanosystems Research, Austrian Academy of Sciences, Graz, Austria.
authors: Beate
authors: B
authors: Boulgaropoulos
authors: Michael
authors: M
authors: Rappolt
authors: Barbara
authors: B
authors: Sartori
authors: Heinz
authors: H
authors: Amenitsch
authors: Georg
authors: G
authors: Pabst
mesh_terms: D002518:Ceramides / Q000737:chemistry*; D003198:Computer Simulation; D008560:Membrane Fluidity; D008563:Membrane Lipids / Q000737:chemistry*; D021962:Membrane Microdomains / Q000737:chemistry* / Q000648:ultrastructure; D008565:Membrane Proteins / Q000737:chemistry* / Q000648:ultrastructure; D008956:Models, Chemical; D008958:Models, Molecular
chemical_list: D002518:Ceramides; D008563:Membrane Lipids; D008565:Membrane Proteins