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. 2021 May 9;18(1):171–190. doi: 10.1080/15548627.2021.1922982

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© 2021 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group.

This is an Open Access article distributed under the terms of the Creative Commons Attribution-NonCommercial-NoDerivatives License (http://creativecommons.org/licenses/by-nc-nd/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited, and is not altered, transformed, or built upon in any way.

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Figure 7. — UBX domain of UBXN1 mediates interaction with PRKN. (A) Schematic depicting the domain organization of UBXN1 and mutants of UBXN1 used in this study. (B) HeLa cells transfected with expression plasmids for mitoDsRed, YFP-PRKN and FLAG-UBXN1 (not shown) FLAG-UBXN1ΔUBX or FLAG-UBXN1ΔUBA were treated with 25 µM CCCP for 6 h or left untreated as control. Cells were fixed, stained using mouse anti-FLAG antibodies and analyzed by confocal microscopy. Representative images obtained from three independent experiments are displayed. Scale bar: 20 µm. (C) Mitochondrial translocation of YFP-PRKN was assessed by correlating PRKN and mitoDsRed distribution (Pearson’s correlation) in confocal images from B. Boxplots represent three independent experiments with at least 30 cells per condition. No statistical significant difference between treatment groups was found by unbalanced one-way ANOVA. (D) Immunoprecipitation using anti-GFP antibodies were performed on whole cell lysates (WCL) of HeLa cells transfected with expression plasmids for either YFP-PRKN or mCherry-PRKN and FLAG-UBXN1ΔUBX or FLAG-UBXN1ΔUBA. WCLs, immunopurified and co-purifying proteins were analyzed by western blotting using anti-GFP and anti-UBXN1 antibodies respectively. Due to their size difference, western blots of 9% and 12% SDS-PAGE for analysis of FLAG-UBXN1ΔUBX or FLAG-UBXN1ΔUBA co-purification are shown.