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. 2022 Sep 19;144(5):881–910. doi: 10.1007/s00401-022-02491-8

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© The Author(s) 2022

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/.

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Fig. 7 — Hypothetical model of STI1 regulation of toxic α-synuclein and promotion of phosphorylation at S129. 1 Toxic α-synuclein species disturb chaperome and contribute to protein misfolding stress. 2 The TPR2A domain of STI1 interacts with the C-terminal domain of α-synuclein forming a complex in the brain. 3 The STI1-α-synuclein interaction may facilitate α-synuclein phosphorylation at S129. 4 STI1 may scaffold α-synuclein to deliver it to Hsp90. 5 STI1 and Hsp90 are sequestered into inclusions in multiple brain regions. Thus, α-synuclein function and potential to aggregate may depend on different chaperones and their co-chaperones in specific cell types. These toxic effects lead to white matter atrophy, cognitive, and motor deficits. Figure designed with BioRender.com software