Cooperative Recruitment of Dynamin and BIN/Amphiphysin/Rvs (BAR) Domain-containing Proteins Leads to GTP-dependent Membrane Scission |
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| Authors: | Michael Meinecke Emmanuel Boucrot Gamze Camdere Wai-Ching Hon Rohit Mittal Harvey T McMahon |
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| Institution: | From the ‡Laboratory of Molecular Biology, Medical Research Council, Hills Road, Cambridge, CB2 0QH, United Kingdom.;the §Department for Biochemistry II, Georg-August-University Göttingen, 37073 Göttingen, Germany, and ;¶Institute of Structural and Molecular Biology, Division of Biosciences, University College London, London WC1E 6BT, United Kingdom |
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| Abstract: | Dynamin mediates various membrane fission events, including the scission of clathrin-coated vesicles. Here, we provide direct evidence for cooperative membrane recruitment of dynamin with the BIN/amphiphysin/Rvs (BAR) proteins, endophilin and amphiphysin. Surprisingly, endophilin and amphiphysin recruitment to membranes was also dependent on binding to dynamin due to auto-inhibition of BAR-membrane interactions. Consistent with reciprocal recruitment in vitro, dynamin recruitment to the plasma membrane in cells was strongly reduced by concomitant depletion of endophilin and amphiphysin, and conversely, depletion of dynamin dramatically reduced the recruitment of endophilin. In addition, amphiphysin depletion was observed to severely inhibit clathrin-mediated endocytosis. Furthermore, GTP-dependent membrane scission by dynamin was dramatically elevated by BAR domain proteins. Thus, BAR domain proteins and dynamin act in synergy in membrane recruitment and GTP-dependent vesicle scission. |
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| Keywords: | Endocytosis Membrane Membrane Biophysics Membrane Reconstitution Membrane Trafficking |
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