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Generation of high curvature membranes mediated by direct endophilin bilayer interactions
Open accessAbstract
Endophilin 1 is a presynaptically enriched protein which binds the GTPase dynamin and the polyphosphoinositide phosphatase synptojanin. Perturbation of endophilin function in cell-free systems and in a living synapse has implicated endophilin in endocytic vesicle budding (Ringstad, N., H. Gad, P. Low, G. Di Paolo, L. Brodin, O. Shupliakov, and P. De Camilli. 1999. Neuron. 24:143–154; Schmidt, A., M. Wolde, C. Thiele, W. Fest, H. Kratzin, A.V. Podtelejnikov, W. Witke, W.B. Huttner, and H.D. Soling. 1999. Nature. 401:133–141; Gad, H., N. Ringstad, P. Low, O. Kjaerulff, J. Gustafsson, M. Wenk, G. Di Paolo, Y. Nemoto, J. Crun, M.H. Ellisman, et al. 2000. Neuron. 27:301–312). Here, we show that purified endophilin can directly bind and evaginate lipid bilayers into narrow tubules similar in diameter to the neck of a clathrin-coated bud, providing new insight into the mechanisms through which endophilin may participate in membrane deformation and vesicle budding. This property of endophilin is independent of its putative lysophosphatydic acid acyl transferase activity, is mediated by its NH2-terminal region, and requires an amino acid stretch homologous to a corresponding region in amphiphysin, a protein previously shown to have similar effects on lipid bilayers (Takei, K., V.I. Slepnev, V. Haucke, and P. De Camilli. 1999. Nat. Cell Biol. 1:33–39). Endophilin cooligomerizes with dynamin rings on lipid tubules and inhibits dynamin's GTP-dependent vesiculating activity. Endophilin B, a protein with homology to endophilin 1, partially localizes to the Golgi complex and also deforms lipid bilayers into tubules, underscoring a potential role of endophilin family members in diverse tubulovesicular membrane-trafficking events in the cell.
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Maxfield, F. R., & McGraw, T. E. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1315 · Cited by 1,729
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Peter, B. J., Kent, H. M., Mills, I. G., Vallis, Y., Butler, P. J. G., Evans, P. R., & McMahon, H. T. (2004) · Science · doi:10.1126/science.1092586 · Cited by 1,636
Membrane recognition by phospholipid-binding domains
Lemmon, M. A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2328 · Cited by 1,419
Mitochondrial dynamics and apoptosis
Suen, D.-F., Norris, K. L., & Youle, R. J. (2008) · Genes & Development · doi:10.1101/gad.1658508 · Cited by 1,270
Curvature of clathrin-coated pits driven by epsin
Ford, M. G. J., Mills, I. G., Peter, B. J., Vallis, Y., Praefcke, G. J. K., Evans, P. R., & McMahon, H. T. (2002) · Nature · doi:10.1038/nature01020 · Cited by 1,019
Endocytosis by random initiation and stabilization of clathrin-coated pits
Ehrlich, M., Boll, W., van Oijen, A., Hariharan, R., Chandran, K., Nibert, M. L., & Kirchhausen, T. (2004) · Cell · doi:10.1016/j.cell.2004.08.017 · Cited by 843
The Machines that Divide and Fuse Mitochondria
Hoppins, S., Lackner, L., & Nunnari, J. (2007) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.76.071905.090048 · Cited by 790
The BAR Domain Superfamily: Membrane-Molding Macromolecules
Frost, A., Unger, V. M., & De Camilli, P. (2009) · Cell · doi:10.1016/j.cell.2009.04.010 · Cited by 574
Self-citationSaheki, Y., & De Camilli, P. (2012) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a005645 · Cited by 457
ITOH, T., & DECAMILLI, P. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids · doi:10.1016/j.bbalip.2006.06.015 · Cited by 361
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Soukup, S.-F., Kuenen, S., Vanhauwaert, R., Manetsberger, J., Hernández-Díaz, S., Swerts, J., Schoovaerts, N., Vilain, S., Gounko, N. V., Vints, K., et al. (2016) · Neuron · doi:10.1016/j.neuron.2016.09.037 · Cited by 293
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Hui, E., Johnson, C. P., Yao, J., Dunning, F. M., & Chapman, E. R. (2009) · Cell · doi:10.1016/j.cell.2009.05.049 · Cited by 291
Habermann, B. (2004) · The EMBO Reports · doi:10.1038/sj.embor.7400105 · Cited by 281
Lipowsky, R. (2013) · Faraday Discuss. · doi:10.1039/c2fd20105d · Cited by 270
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Goff, S. P. (2007) · Nature Reviews Microbiology · doi:10.1038/nrmicro1541 · Cited by 247
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Wang, Q., Navarro, M. V. A. S., Peng, G., Molinelli, E., Lin Goh, S., Judson, B. L., Rajashankar, K. R., & Sondermann, H. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0902974106 · Cited by 200
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Prokic, I., Cowling, B. S., & Laporte, J. (2014) · Journal of Molecular Medicine · doi:10.1007/s00109-014-1138-1 · Cited by 188
Bennett, A. E., Narayan, K., Shi, D., Hartnell, L. M., Gousset, K., He, H., Lowekamp, B. C., Yoo, T. S., Bliss, D., Freed, E. O., et al. (2009) · PLoS Pathogens · doi:10.1371/journal.ppat.1000591 · Cited by 163
Meinecke, M., Boucrot, E., Camdere, G., Hon, W.-C., Mittal, R., & McMahon, H. T. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.444869 · Cited by 155
Molecular basis for SH3 domain regulation of F-BAR–mediated membrane deformation
Rao, Y., Ma, Q., Vahedi-Faridi, A., Sundborger, A., Pechstein, A., Puchkov, D., Luo, L., Shupliakov, O., Saenger, W., & Haucke, V. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003478107 · Cited by 149
Usami, Y., Popov, S., & Göttlinger, H. G. (2007) · Journal of Virology · doi:10.1128/jvi.00314-07 · Cited by 143
Muller, A. J., Baker, J. F., DuHadaway, J. B., Ge, K., Farmer, G., Donover, P. S., Meade, R., Reid, C., Grzanna, R., Roach, A. H., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.12.4295-4306.2003 · Cited by 139
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Aguilar, R. C., & Wendland, B. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00010-3 · Cited by 138
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Watanabe, S., Mamer, L. E., Raychaudhuri, S., Luvsanjav, D., Eisen, J., Trimbuch, T., Söhl-Kielczynski, B., Fenske, P., Milosevic, I., Rosenmund, C., et al. (2018) · Neuron · doi:10.1016/j.neuron.2018.06.005 · Cited by 131
Jović, M., Kieken, F., Naslavsky, N., Sorgen, P. L., & Caplan, S. (2009) · Molecular Biology of the Cell · doi:10.1091/mbc.e08-11-1102 · Cited by 81
Casal, E., Federici, L., Zhang, W., Fernandez-Recio, J., Priego, E.-M., Miguel, R. N., DuHadaway, J. B., Prendergast, G. C., Luisi, B. F., & Laue, E. D. (2006) · Biochemistry · doi:10.1021/bi060717k · Cited by 77
Tang, X., Germain, B. S., & Lee, W.-L. (2012) · Journal of Cell Biology · doi:10.1083/jcb.201112017 · Cited by 56
Yoon, Y., Zhang, X., & Cho, W. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.372789 · Cited by 47
Wu, T., & Baumgart, T. (2014) · Biochemistry · doi:10.1021/bi501082r · Cited by 47
A Rugged Energy Landscape Mechanism for Trapping of Transmembrane Receptors during Endocytosis
Licht, S. S., Sonnleitner, A., Weiss, S., & Schultz, P. G. (2003) · Biochemistry · doi:10.1021/bi026059v · Cited by 22
Metadata
- Authors
- Farsad, K., Ringstad, N., Takei, K., Floyd, S. R., Rose, K., & De Camilli, P.
- Venue
- The Journal of Cell Biology
- Publisher
- Rockefeller University Press
- Published
- 2001-10-15
- Volume
- 155
- Issue
- 2
- Pages
- 193-200
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- OpenAlex
- W2071877471
- Cited by
- 603
- References
- 0
- FWCI
- 11.74
- Type
- journal article
- Language
- en
- Open access
- green
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