Membrane-bending mechanism of amphiphysin N-BAR domains.
BAR domains are highly conserved protein domains participating in a diversity of cellular processes that involve membrane remodeling. The mechanisms underlying such remodeling are debated. For the relatively well-studied case of amphiphysin N-BAR domain, one suggested mechanism involves scaffolding, i.e., binding of a negatively charged membrane to the protein's positively charged curved surface. An alternative mechanism suggests that insertion of the protein's N-terminal amphipathic segments (N-helices H0) into the membrane leads to bending. Here, we address the issue through all-atom and coarse-grained simulations of multiple amphiphysin N-BAR domains and their components interacting with a membrane. We observe that complete N-BAR domains and BAR domains without H0s bend the membrane, but H0s alone do not, which suggests that scaffolding, rather than helix insertion, plays a key role in membrane sculpting by amphiphysin N-BAR domains.
Arkhipov
Anton
A
Department of Physics and Beckman Institute, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
Yin
Ying
Y
Schulten
Klaus
K
D000818:Animals; D003198:Computer Simulation; D004330:Drosophila; D029721:Drosophila Proteins / Q000737:chemistry*; D008051:Lipid Bilayers / Q000737:chemistry*; D008956:Models, Chemical; D008958:Models, Molecular; D009419:Nerve Tissue Proteins / Q000737:chemistry*; D010713:Phosphatidylcholines / Q000737:chemistry; D013997:Time Factors
D029721:Drosophila Proteins; D008051:Lipid Bilayers; D009419:Nerve Tissue Proteins; D010713:Phosphatidylcholines; C075637:amphiphysin; C017251:1,2-oleoylphosphatidylcholine