Abstract
The ability of cells to maintain and change the shapes of their membranes is vital for many cellular processes. Peripheral membrane proteins in the BAR (Bin/amphiphysin/Rvs) superfamily have been identified as membrane remodelers involved in cellular trafficking. Their membrane deformation abilities can be attributed to their intrinsically curved molecular shape. In addition, formation of oligomers in ordered arrays also aid in stabilization of curved membranes. However, changes in membrane topology also depend on mechanical properties of the bilayer, which in turn are influenced by factors such as temperature and lipid compositions. Using negative stain electron microscopy, we show that by altering these not-so-subtle membrane properties, we observe differences in the membrane deformation activities of several BAR domain proteins. Our results provide a systematic and unbiased approach towards understanding the general mechanisms underlying membrane deformation mediated by BAR superfamily proteins, and in particular the role of membrane properties in this process.
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