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. 2022 May 6;5:423. doi: 10.1038/s42003-022-03377-x

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© The Author(s) 2022

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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Fig. 6 — a Schematic of the organization of wild type MFN2 and MFN2(ΔTM). G domain, GTPase domain; HD1/2, helical domain 1/2; T, transmembrane region; L, a Gly-Ser linker. Amino acids 606–647 in wild-type MFN2 were replaced with a 10 amino acid linker GGSGGGSGGG. b Confocal micrographs of HeLa cells transfected with FLAG-tagged MFN2(ΔTM). Cells were immunostained for endogenous ABCD3 (Alexa Fluor 647) and FLAG (Alexa Fluor 555). Representative confocal micrographs of HeLa cells transfected with (d) or without (c) MFN2(ΔTM)-FLAG. MFN2-EGFP was overexpressed to induce mitochondrion-peroxisome clustering in both conditions. Cells were stained for ABCD3 and MFN2(ΔTM)-FLAG. e The statistics of cell numbers in different stages were analyzed for experiments in c (n = 240 cells) and d (n = 106 cells).