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. 2022 Feb 14;10:22. doi: 10.1186/s40478-022-01322-x

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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/. 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. 3 — Molecular chaperones are sequestered by cytoplasmic poly-GA aggregates. A Co-expression of mCherry-tagged poly-GA and EGFP-tagged chaperones and adapter proteins shows the tight association of SQSTM1, UBXN6, VCP, and HSPA8 within the periphery of dense cytoplasmic poly-GA aggregates. B Endogenous BAG3, SQSTM1, UBXN6, VCP, and HSPA8 proteins are sequestered around EGFP-tagged poly-GA aggregates, disrupting their normal endogenous staining pattern. Scale bar: 5 µm