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. 2018 Oct 24;8:15726. doi: 10.1038/s41598-018-33879-w

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© The Author(s) 2018

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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Schematic diagram depicting the proposed mechanism of action of fisetin: SPR studies showed that interaction of fisetin with RSK2 promotes its binding to YB-1. Fisetin mediated downregulation of YB-1/RSK signaling is associated with a decrease in MDR1. Fisetin-treated cells showed an initial increase in ERK1/2 phosphorylation at threonine²⁰²/tyrosine²⁰⁴ followed by a sustained decrease, suggestive of a biphasic response. Fisetin mediated decrease in RSK/YB-1 is independent of ERK. Inhibition of ERK did not interfere with RSK phosphorylation at threonine³⁵⁹/serine³⁶³ residues in fisetin-treated cells. However, fisetin mediated increase in RSK serine³⁸⁰ phosphorylation was abrogated with ERK inhibition suggesting that ERK was driving phosphorylation at this residue.