TCB Publications - Abstract

Anton Arkhipov, Ying Yin, and Klaus Schulten. Membrane-bending mechanism of amphiphysin N-BAR domains. Biophysical Journal, 97:2727-2735, 2009. (PMC: 2776244)

ARKH2009B 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 proteinís positively charged curved surface. An alternative mechanism suggests that insertion of the proteinís 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 segments interacting with a membrane. We observe that 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.


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