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. 2017 Sep 6;7:10744. doi: 10.1038/s41598-017-11008-3

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© The Author(s) 2017

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as 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. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Cardiolipin interactions trigger active Drp1 assembly. (a) A model illustrates the Drp1 architecture on a GC/PS template. Stalk and 80 loop (purple) G-domain dimerization drive helical assembly. (b) A separate model illustrates the Drp1 architecture on a GC/CL template. Stalk and distinct G-domain dimerizations near the GTP binding pocket (orange) promote assembly of a more active polymer in the presence of CL. (c) On a GC/PS template, the variable domain of Drp1 interacts weakly with the membrane surface. (d) On a GC/CL template, the variable domain is stabilized on the membrane surface, which induces a pivot at the stalk interface to transmit a specific lipid signal at the membrane to the peripheral G domains where an activate conformation is formed. (e) A model depicts Drp1 interactions with CL at the surface of mitochondria where this unique lipid activates Drp1 function at defined sites primed for mitochondrial fission.