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. 2024 Jan 1;33(1):e4840. doi: 10.1002/pro.4840

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© 2023 The Authors. Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.

This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made.

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XRK2F2 binds to the ZZ domain and increases the interaction between p62/SQSTM1 and LC3. (a) The compound XRK2F2 increases the interaction between purified His‐Trx‐p62/SQSTM1 A/A (His‐Trx‐p62 A/A) and GST‐LC3. Results expressed as mean ± SD with *p < 0.05 by unpaired t‐test. (b) Non purified FLAG‐p62/SQSTM1 wt (wild type sequence) interacts with LC3B on the modified AlphaScreen assay. Data are representative of two independent experiments. (c) XRK2F2 increases the interaction between FLAG‐p62/SQSTM1 wt and GST‐LC3 in the context of the cell lysate. Data are representative of two independent experiments. (d) Change in the thermal stability of the purified ZZ domain due to the binding of XRK2F2. Graphic depicts three replicates of three independent experiments. Results are expressed as Mean ± SD with **p < 0.01 and ***p = 0.0001 by one‐way ANOVA followed by Bonferroni multiple comparison test. (A, C) The binding (%) was calculated considering the DMSO condition as 100%.