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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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Removal of the variable domain (VD) abolishes Drp1 oligomerization with CL nanotubes. (a) Sedimentation was measured to assess the oligomeric state of wild-type (WT, black) and ΔVD (grey) Drp1 alone, in the presence of GMPPCP, in the presence of CL nanotubes (GC/CL) and in the presence of CL nanotubes with GMPPCP (GC/CL + PCP). Representative supernatant (S) and pellet (P) gel samples are shown. (b) A representative cryo-EM image demonstrates WT Drp1 decoration of the GC/CL nanotube in the presence of GMPPCP, the arrowheads indicate rungs of the protein helix. (c) Under the same conditions ΔVD did not decorate the nanotubes. Scale bar, 100 nm. Insets display the boxed region on the micrograph. Scale bar, 50 nm.