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. 2021 Oct 5;81(2):243–254. doi: 10.1136/annrheumdis-2021-221010

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© Author(s) (or their employer(s)) 2022. Re-use permitted under CC BY. Published by BMJ.

This is an open access article distributed in accordance with the Creative Commons Attribution 4.0 Unported (CC BY 4.0) license, which permits others to copy, redistribute, remix, transform and build upon this work for any purpose, provided the original work is properly cited, a link to the licence is given, and indication of whether changes were made. See: https://creativecommons.org/licenses/by/4.0/.

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The novel E3 ligase MKRN4 induces proteasomal degradation of GLK. (A) Immunoblotting of Flag-tagged GLK (anti-FLAG), Myc-tagged MKRN4 (anti-MYC) and tubulin proteins from Jurkat T cells cotransfected with Flag-GLK plus increasing amounts of Myc-MKRN4 plasmids. (B) Immunoblotting of Flag-tagged GLK (anti-FLAG), Myc-tagged MKRN4 (anti-MYC) and tubulin proteins from HEK293T cells cotransfected with Flag-GLK plus increasing amounts of Myc-MKRN4 plasmids. (C) Immunoblotting of Flag-tagged GLK (anti-FLAG), Myc-tagged MKRN4 (anti-MYC) and tubulin proteins from HEK293T cells cotransfected with Flag-GLK plus Myc-MKRN4 plasmids. Cells were treated with 25 µM MG132 for 2 hours before being harvested. (D) In situ PLA assays of the interaction between Myc-tagged MKRN4 and Flag-tagged GLK proteins in HEK293T cells. Cells were treated with 25 µM MG132 for 2 hours before being harvested. Nuclei were stained with 4′,6-diamidino-2-phenylindole (DAPI). Imaging was detected by Leica DM2500 upright fluorescence microscope. Original magnification, ×200. scale bars, 50 µm. PLA, proximity ligation assay.