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. 2020 May 22;11:2592. doi: 10.1038/s41467-020-16335-0

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© The Author(s) 2020

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. 8 — a Confocal microscopy images of YFP-Rab32 (green) localized around mitochondria (red) and b colocalized with Dosmit (red) in fly muscle tissue. Scale bars: 10 μm. c Tom20-HA (red) ectopically expressed and colocalized with YFP-Rab32 (green). d Western blotting of flight-muscle tissue homogenates showed expression of the YFP-Rab32 protein in the mitochondrial fraction only (M: mitochondrial fraction; C: cytosolic fraction; Tubulin: cytosolic control; Porin: mitochondrial control). S2 cells transfected with Hsc70-5-HA or Rab32-HA plasmids. e When Rab32-HA or Hsc70-5-HA is immunoprecipitated with an anti-HA antibody, Dosmit can be detected in the Rab32-bound complex. f When endogenous Dosmit proteins are immunoprecipitated with the anti-Dosmit antibody, only Rab32-HA can be detected in the Dosmit–pulled-down complex. For the pull-down, 10 μg of input was loaded. For SDS-PAGE, 500 μg protein from the immunoprecipitation was loaded. Source data are provided as a Source data file.