期刊
BIOPHYSICAL JOURNAL
卷 97, 期 10, 页码 2727-2735出版社
CELL PRESS
DOI: 10.1016/j.bpj.2009.08.051
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资金
- National Institutes of Health [P41-RR005969, R01-GM067887]
- National Science Foundation [PHY0822613, MCA93S028]
- Office of Science of the U.S. Department of Energy [DE-AC02-06CH11357]
- Direct For Mathematical & Physical Scien
- Division Of Physics [0822613] Funding Source: National Science Foundation
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.
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