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. 2021 Apr 28;40:144. doi: 10.1186/s13046-021-01950-6

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© The Author(s) 2021

Open AccessThis 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 licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence 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 licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

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Fig. 2 — Biological responses triggered after the recognition of TNKS1/2 substrates. Tankyrases recognize their binding partners via the ANK domain. The most studied function of TNKS1/2 is the regulation of protein stability via proteasomal degradation. Tankyrases PARylate many substrates like Axin1/2, PTEN or 3BP2 and then, the E3 ubiquitin ligase RNF146 recognizes the PARylated proteins and adds a poly-ubiquitin chain linked by its Lys48 residues, which trigger their proteasomal degratation (a). More recently, LKB1 was shown to interact with TNKS1/2 and RNF146, but in this case, tankyrase is able to PARylate LKB1 and RNF146 adds a poly-ubiquitin chain linked by Lys63 in orde to disrupt the complex formed by LKB1, STRAD and MO25 (b). The interaction between tankyrase and the proteins GMD and Mcl-1 causes the inhibition of the catalytic activity of TNKS1/2 (c). Tankyrases also can work as scaffolding proteins via their ANK domain, promoting the interaction between different proteins like PEX14 and ATG9 (without PARylation) or MERIT40 (low levels of PAR) (d)