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. 2017 Jul 17;7:5519. doi: 10.1038/s41598-017-05736-9

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© The Author(s) 2017

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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Identification of phosphoproteins phosphorylated by excessive ROS1 signaling. (A,B) Volcano plot indicates log2-fold-change in values (horizontal axis) of phosphopeptides in F2004V- or F2075C-mutated cells without cabozantinib and cabozantinib-treated (100 nM) wild-type CD74-ROS1 cells, against the −log10 p value (vertical axis). These plots indicate the log2 fold-change between upregulated or downregulated phosphopeptides in F2004V- (A) or F2075C- (B) mutated cells by cabozantinib removal (F2004V or F2075C cells without/with 10 nM cabozantinib, respectively) and upregulated or downregulated phosphopeptides in wild-type CD74-ROS1 cell (untreated/cabozantinib-treated). Each plot is based on the mean fold-change of value and the p value of two independent experiments. Plots which passed the 0.05-Benjamini-Hochberg-false discovery rate threshold are shown in red. (C) List of representative common phosphopeptides which were significantly upregulated in the F2004V- or F2075C-mutated cells after removal of cabozantinib. (D) Coomassie brilliant blue-stained gel (right) and autoradiography (left) of human ROS1 and FAF1 proteins electrophoresed with [gamma-³²P] ATP. Uncropped gel and autoradiograph are presented in Supplementary Fig. S11.