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. 2019 Nov 5;9:16014. doi: 10.1038/s41598-019-52408-x

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© The Author(s) 2019

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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p62 directly interacts with Tax through its 170-206 domain. (a) GST and GST-tagged p62 were expressed in bacteria and used for GST pulldown of in vitro translated ³⁵S-labeled Tax. Inputs as well as eluates were run on SDS-PAGE gels and autoradiography was performed. (b) Domain organization of p62 constructs with different deletion used for GST and MBP pulldown assays. The results of the pulldown assays shown in (c,d) indicate Tax binding ability and are indicated on the right. PB1, Phox and Bem1 domain; ZZ, zinc finger domain; MIR, multiple protein interaction region; LIR, LC3-interacting region; KIR, KEAP1 interacting region; UBA, ubiquitin-associated domain. (c,d) GST pulldown (c) and MBP pulldown assays (d) were performed with different p62 constructs. The percentage of input radioactively labeled-Tax bound to p62 was quantified from three independent experiments. CBB, Coomassie brilliant blue-stained SDS-PAGE gel.