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. 2023 Nov 8;13:19383. doi: 10.1038/s41598-023-46614-x

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© The Author(s) 2023

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 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/.

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Phosphorylation of Thr55 does not change local conformation but may affect the interaction between α5-subunit and proteins. (A) Representation of part of the three-dimensional structure of the 20S proteasome (pdb 3D29) focused on the region where the Thr55 residue susceptible to phosphorylation is located. The structure with dephosphorylated Thr55 is shown in pink while the simulated structure with phospho-Thr55 in represented in blue. (B) Representation of models of interaction between the 20S proteasome α-ring and α-synuclein. The models were generated with the Haddock program. Interaction of α-synuclein with the proteasome α-ring in the absence or presence of Thr55 phosphorylation is represented in blue and red, respectively. Phosphorylated threonine 55 is shown in yellow.