Membrane-bending mechanism of amphiphysin N-BAR domains

Anton Arkhipov, Ying Yin, Klaus Schulten

Research output: Contribution to journalArticlepeer-review


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.

Original languageEnglish (US)
Pages (from-to)2727-2735
Number of pages9
JournalBiophysical journal
Issue number10
StatePublished - Nov 15 2009

ASJC Scopus subject areas

  • Biophysics


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