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. 2017 Feb 27;74(13):2413–2438. doi: 10.1007/s00018-017-2478-0

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© The Author(s) 2017

Open AccessThis article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

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Fig. 3 — Complex between endophilin and EFA6 as regulator in clathrin-mediated endocytosis. The N-BAR domain of the endophilin dimer (dark and light blue overlapping moons representing endophilin monomers) interacts with the Arf6-specific exchange factor (EFA6). The complex exhibits both increased guanine-nucleotide exchange factor (GEF) activity of the EFA6 constituents and increased selectivity of the endophilin dimer for highly curved membrane shapes (yellow) and thereby plays a crucial role in orchestrating the sequential steps (Arf6 activation and selective membrane tubulation) in clathrin-mediated endocytosis [101]