Control of membrane curvature is required in many important cellular processes, including
endocytosis and vesicular trafficking. Endophilin is a bin/amphiphysin/rvs (BAR) domain
protein that induces vesicle formation by promotion of membrane curvature through
membrane binding as a dimer. Using site-directed spin labeling and EPR spectroscopy, we
show that the overall BAR domain structure of the rat endophilin A1 dimer determined
crystallographically is maintained under predominantly vesiculating conditions. Spin-labeled …