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Structural basis of membrane bending by the N-BAR protein endophilin |
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| Authors: | Mim Carsten Cui Haosheng Gawronski-Salerno Joseph A Frost Adam Lyman Edward Voth Gregory A Unger Vinzenz M |
| Affiliation: | 1 Department of Molecular Biosciences, Northwestern University, 2205 Campus Drive, Evanston, IL 60208, USA 2 Chemistry of Life Processes Institute, Northwestern University, 2170 Campus Drive, Evanston, IL 60208, USA 3 Department of Chemistry, Institute for Biophysical Dynamics, James Franck Institute, and Computation Institute, University of Chicago, 5735 South Ellis Avenue, Chicago, IL 60637, USA 4 Department of Physics and Astronomy and Department of Chemistry and Biochemistry, University of Delaware, Newark, DE 19716, USA 5 Department of Biochemistry, University of Utah, 15 North Medical Drive East, Salt Lake City, UT 84112, USA |
| Abstract: | Functioning as key players in cellular regulation of membrane curvature, BAR domain proteins bend bilayers and recruit interaction partners through poorly understood mechanisms. Using electron cryomicroscopy, we present reconstructions of full-length endophilin and its N-terminal N-BAR domain in their membrane-bound state. Endophilin lattices expose large areas of membrane surface and are held together by promiscuous interactions between endophilin's amphipathic N-terminal helices. Coarse-grained molecular dynamics simulations reveal that endophilin lattices are highly dynamic and that the?N-terminal helices are required for formation of a stable and regular scaffold. Furthermore, endophilin accommodates different curvatures through?a quantized addition or removal of endophilin dimers, which in some cases causes dimerization of endophilin's SH3 domains, suggesting that the spatial presentation of SH3 domains, rather than affinity, governs the recruitment of downstream interaction partners. |
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