Interplay between cellular membranes and their peripheral proteins drives many processes in eukaryotic cells. Proteins of the Bin/Amphiphysin/Rvs (BAR) domain family, in particular, play a role in cellular morphogenesis, for example curving planar membranes into tubular membranes. However, it is still unclear how F-BAR domain proteins act on membranes. Electron microscopy revealed that, in vitro, F-BAR proteins form regular lattices on cylindrically deformed membrane surfaces. Using all-atom and coarse-grained (CG) molecular dynamics simulations, we show that such lattices, indeed, induce tubes of observed radii. A 250 ns all-atom simulation reveals that F-BAR domain curves membranes via the so-called "scaffolding" mechanism. Plasticity of the F-BAR domain permits conformational change in response to membrane interaction, via partial unwinding of the domain's 3-helix bundle structure. A CG simulation covering more than 350 us provides a dynamic picture of membrane tubulation by lattices of F-BAR domains. A series of CG simulations identified the optimal lattice type for membrane sculpting, which matches closely the lattices seen through cryo-electron microscopy.

Hang Yu currently holds a BS with Honors, Biology/Computing, 2007 from Nanyang Technological University, Singapore. He is pursuing graduate studies in BioPhysics at the University of Illinois with an interest in BAR domains.

Researchers should cite this work as follows:

• Hang Yu (2012), "[Illinois] Beckman Graduate Seminar: Membrane Sculpting by F-BAR Domains Studied by Molecular Dynamics Simulations," https://nanohub.org/resources/16098.

  BibTex | EndNote

1. BAR Domain
2. Beckman Institute
3. Illinois
4. Membrane Sculpting
5. molecular dynamics (MD)
6. NanoBio Node at Illinois
7. nanohub