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. 2020 Jun 17;10:9849. doi: 10.1038/s41598-020-66750-y

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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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DYRK1A-E396ter is degraded by the ubiquitin-mediated proteasomal pathway and is intrinsically inactive. (a) FLAG-tagged DYRK1A-WT, DYRK1A-E396ter, and DYRK1A-K188R plasmids were transiently co-expressed with Tau protein in 293 T cells for 24 h. Total cell extracts were harvested and subjected to western blotting with anti-FLAG, anti-phosphorylated-Tau (at T212, p-Tau), and anti-Tau antibodies. HnRNP A1 served as a loading control. Asterisks indicate nonspecific proteins. (b) FLAG-tagged DYRK1A-WT and DYRK1A-E396ter were co-expressed with Tau protein and then treated with selective proteolytic pathway inhibitors: MG132 for the proteasome, NH₄Cl for lysosome, calpeptin for calpain, and 3-methyladenine for autophagy. (c) FLAG-DYRK1A-E396ter and HA-ubiquitin were co-expressed for 24 h prior to MG132 treatment (10 μM, 11 h). Total cell extracts were harvested, FLAG-DYRK1A-E396ter was immunoprecipitated with anti-FLAG antibody, and polyubiquitination was detected by western blotting with an anti-HA antibody. Uncropped full-sized blots are presented in Supplementary Fig. S4.