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

Research output: Contribution to journalArticlepeer-review

54 Scopus citations


Cellular membranes are continuously remodeled. Te crescent-shaped bin-amphiphysin-rvs (BAR) domains remodel membranes in multiple cellular pathways. Based on studies of isolated BAR domains in vitro, the current paradigm is that BAR domain-containing proteins polymerize into cylindrical scaffolds that stabilize lipid tubules. But in nature, proteins that contain BAR domains ofen also contain large intrinsically disordered regions. Using in vitro and live cell assays, here we show that full-length BAR domain-containing proteins, rather than stabilizing membrane tubules, are instead surprisingly potent drivers of membrane fssion. Specifcally, when BAR scaffolds assemble at membrane surfaces, their bulky disordered domains become crowded, generating steric pressure that destabilizes lipid tubules. More broadly, we observe this behavior with BAR domains that have a range of curvatures. Tese data suggest that the ability to concentrate disordered domains is a key driver of membrane remodeling and fssion by BAR domain-containing proteins.

Original languageEnglish (US)
Pages (from-to)664-682
Number of pages19
JournalJournal of Cell Biology
Issue number2
StatePublished - Feb 1 2019

ASJC Scopus subject areas

  • Cell Biology


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