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_37
Snippet: The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/276147 doi: bioRxiv preprint (Henne et al., 2010; Ma et al., 2016) . However, previous work showed that FCHo2 is present throughout the lifetime of clathrin-coated pits (Taylor et al., 2011) , supporting the possible role of FCHo2 in membrane shaping. Moreover, many F-BAR proteins involved in other cellular pathways such as cytokin.....
Document: The copyright holder for this preprint (which was not peer-reviewed) is the author/funder. . https://doi.org/10.1101/276147 doi: bioRxiv preprint (Henne et al., 2010; Ma et al., 2016) . However, previous work showed that FCHo2 is present throughout the lifetime of clathrin-coated pits (Taylor et al., 2011) , supporting the possible role of FCHo2 in membrane shaping. Moreover, many F-BAR proteins involved in other cellular pathways such as cytokinesis also contain large regions of intrinsic disorder (McDonald et al., 2016; Meitinger et al., 2011; . As such, our findings raise the question of whether F-BAR scaffolds facilitate membrane fission in a variety of contexts beyond membrane traffic.
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