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- W2082487911 abstract "We explore changes in curvature in vesicles composed of a mixture of phospholipids and cholesterol upon the binding of protein to the membrane. Experiments were done with model peptides and with members of the BAR family of proteins. Vesicles were prepared using electroformation with a mix of phosphatidylcholine, cholesterol, and sphingomyelin. As a sample is lowered through temperature Tmix, a homogeneous vesicle phase separates into two fluid phases with distinct compositions. A line tension at the boundary between the phases deforms the membrane, producing buds with a shape determined by a balance of membrane and line tension. Green fluorescent protein (GFP) with a 6X histidine tag was added to the solution, where it bound to Ni-chelating phospholipids present in the membrane at concentrations ranging from 0.1 to 5 mol%. Domain budding was recorded before and after GFP addition using both differential interference and fluorescence microscopy. Analysis of the shape of the vesicle before and after addition of GFP allows for the determination of the change in line tension owing to the GFP binding. Similar results were obtained with vesicles introduced to poly-L-histidine. A possible mechanism for the change in shape seen with both GFP and poly-L-histidine binding is formation of protein-Ni-chelating lipid complexes that sit at the boundary between phases and lower the line tension. Preliminary investigations into shape changes caused by BAR domains of Drosophila amphiphysin revealed fine vesicle tubulation that initiated at the boundary between the two lipid phases. The addition of both model proteins (GFP and poly-L-histidine) and biologically relevant protein (BAR domains) into our system allows for a broader understanding of the effect of protein, which are ubiquitous in cell membranes, on phase separation and budding.NSF IGERT Program in NanotechnologyUmass Biomedical Innovation Initiative" @default.
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- W2082487911 date "2010-01-01" @default.
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- W2082487911 title "Protein-Induced Shape Changes in Phase-Separated Vesicles" @default.
- W2082487911 doi "https://doi.org/10.1016/j.bpj.2009.12.4250" @default.
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