| | |  | | | | Record from Web of Science® | | | | | | |
| BAR domains as sensors of membrane curvature: The amphiphysin BAR structure |
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| Author(s): Peter BJ, Kent HM, Mills IG, Vallis Y, Butler PJG, Evans PR, McMahon HT |
| Source: SCIENCE Volume: 303 Issue: 5657 Pages: 495-499 Published: JAN 23 2004 |
| Times Cited: 366 References: 46 |
| Abstract: The BAR (Bin/amphiphysin/Rvs) domain is the most conserved feature in amphiphysins from yeast to human and is also found in endophilins and nadrins. We solved the structure of the Drosophila amphiphysin BAR domain. It is a crescent-shaped dimer that binds preferentially to highly curved negatively charged membranes. With its N-terminal amphipathic helix and BAR domain (N-BAR), amphiphysin can drive membrane curvature in vitro and in vivo. The structure is similar to that of arfaptin2, which we find also binds and tubulates membranes. From this, we predict that BAR domains are in many protein families, including sorting nexins, centaurins, and oligophrenins. The universal and minimal BAR domain is a dimerization, membrane-binding, and curvature-sensing module. |
| Document Type: Article |
| Language: English |
| Reprint Address: Evans, PR (reprint author), MRC, Mol Biol Lab, Hills Rd, Cambridge CB2 2QH, England |
Addresses:
1. MRC, Mol Biol Lab, Cambridge CB2 2QH, England |
| Publisher: AMER ASSOC ADVANCEMENT SCIENCE, 1200 NEW YORK AVE, NW, WASHINGTON, DC 20005 USA |
| Subject Category: Multidisciplinary Sciences |
| IDS Number: 765XM |
| ISSN: 0036-8075 |
| DOI: 10.1126/science.1092586 |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |