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 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 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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