Clathrin senses membrane curvature.
| Autor: | Zeno WF; Department of Biomedical Engineering, The University of Texas at Austin, Austin, Texas; Department of Chemical Engineering, The University of Southern California, Los Angeles, California., Hochfelder JB; Department of Biomedical Engineering, The University of Texas at Austin, Austin, Texas., Thatte AS; Department of Biomedical Engineering, The University of Texas at Austin, Austin, Texas., Wang L; Department of Biochemistry, The University of Texas Health Science Center, San Antonio, Texas., Gadok AK; Department of Biomedical Engineering, The University of Texas at Austin, Austin, Texas., Hayden CC; Department of Biomedical Engineering, The University of Texas at Austin, Austin, Texas., Lafer EM; Department of Biochemistry, The University of Texas Health Science Center, San Antonio, Texas., Stachowiak JC; Department of Biomedical Engineering, The University of Texas at Austin, Austin, Texas; Institute for Cellular and Molecular Biology, The University of Texas at Austin, Austin, Texas. Electronic address: jcstach@austin.utexas.edu. |
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| Jazyk: | angličtina |
| Zdroj: | Biophysical journal [Biophys J] 2021 Mar 02; Vol. 120 (5), pp. 818-828. Date of Electronic Publication: 2021 Jan 30. |
| DOI: | 10.1016/j.bpj.2020.12.035 |
| Abstrakt: | The ability of proteins to assemble at sites of high membrane curvature is essential to diverse membrane remodeling processes, including clathrin-mediated endocytosis. Multiple adaptor proteins within the clathrin pathway have been shown to sense regions of high membrane curvature, leading to local recruitment of the clathrin coat. Because clathrin triskelia do not bind to the membrane directly, it has remained unclear whether the clathrin coat plays an active role in sensing membrane curvature or is passively recruited by adaptor proteins. Using a synthetic tag to assemble clathrin directly on membrane surfaces, here we show that clathrin is a strong sensor of membrane curvature, comparable with previously studied adaptor proteins. Interestingly, this sensitivity arises from clathrin assembly rather than from the properties of unassembled triskelia, suggesting that triskelia have preferred angles of interaction, as predicted by earlier structural data. Furthermore, when clathrin is recruited by adaptors, its curvature sensitivity is amplified by 2- to 10-fold, such that the resulting protein complex is up to 100 times more likely to assemble on a highly curved surface compared with a flatter one. This exquisite sensitivity points to a synergistic relationship between the coat and its adaptor proteins, which enables clathrin to pinpoint sites of high membrane curvature, an essential step in ensuring robust membrane traffic. More broadly, these findings suggest that protein networks, rather than individual protein domains, are likely the most potent drivers of membrane curvature sensing. (Copyright © 2021 Biophysical Society. Published by Elsevier Inc. All rights reserved.) |
| Databáze: | MEDLINE |
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