BAR scaffolds drive membrane fission by crowding disordered domains

Wilton T. Snead; Wade F. Zeno; Grace Kago; Ryan W. Perkins; J Blair Richter; Chi Zhao; Eileen M. Lafer; Jeanne C. Stachowiak

The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/276147 doi: bioRxiv preprint mol% DOPC, 5 mol% PtdIns(4,5)P 2 , 15 mol% DOPS, extruded to 200 nm. Membrane composition in tethered vesicle experiments: 76 mol% DOPC, 5 mol% PtdIns(4,5)P 2 , 15 mol% DOPS, 2 mol% Oregon Green 488-DHPE, 2 mol% DP-EG10-biotin, extruded to 200 nm. (A) Representative spinning disc confocal micrographs of GUVs after exposure to 5 µM of either N-BAR (left) or Amph-FL (right). Fluorescence signal comes from Atto 594-labeled protein. (E) Two representative spinning disc confocal micrographs of tethered vesicles before exposure to protein (top) and after exposure to 5 µM N-BAR (bottom). At 5 µM, a higher concentration than used in experiments in Fig. 2 , N-BAR generates membrane tubules with length greater than the diffraction limit of light. Tubules indicated by white arrows. Scale bars: 2 µm. All rights reserved. No reuse allowed without permission.