Selected article for: "BAR ability and steric pressure"
Author: Wilton T. Snead; Wade F. Zeno; Grace Kago; Ryan W. Perkins; J Blair Richter; Chi Zhao; Eileen M. Lafer; Jeanne C. Stachowiak
Title: BAR scaffolds drive membrane fission by crowding disordered domains
  • Document date: 2018_3_4
    • ID: drqseaaa_3
    Snippet: Therefore, we set out to investigate the impact of disordered domains on the membrane remodeling ability of BAR proteins. To our surprise, we found that while isolated BAR domains formed stable membrane tubules, full-length amphiphysin and FCHo1 destabilized these tubules, leading to highly efficient membrane fission. These results challenge the paradigm that BAR scaffolds stabilize membrane tubes, and suggest instead that they act as templates t.....
    Document: Therefore, we set out to investigate the impact of disordered domains on the membrane remodeling ability of BAR proteins. To our surprise, we found that while isolated BAR domains formed stable membrane tubules, full-length amphiphysin and FCHo1 destabilized these tubules, leading to highly efficient membrane fission. These results challenge the paradigm that BAR scaffolds stabilize membrane tubes, and suggest instead that they act as templates that locally amplify steric pressure among disordered domains, leading to membrane fission.

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