Correction to: Quantitative phosphoproteomic analysis reveals reciprocal activation of receptor tyrosine kinases between cancer epithelial cells and stromal fibroblasts

Correction to: Clin Proteom (2018) 15:21 https://doi.org/10.1186/s12014-018-9197-x

Unfortunately, after publication of this article [1], errors were noticed in Figs. 3 and 4. The “T” in the word “pTyr” was missing in Fig. 3. The word “change” was missing after the word “Fold” in the label of y axis in Fig. 4a. The “e” in the word “Co-culture” was missing in Fig. 4a. The correct figures are presented in this correction. The original article has also been updated.

Fig. 3

Phosphotyrosine profiling of cancer epithelial cells and interacting CAFs. a, b Density scatter plot of log₂-transformed phosphopeptide intensity ratios (82T-co-cultured vs. 82T (A) and MDA-MB-231-co-cultured vs. MDA-MB-231) from two SILAC biological experiments. c Pie chart showing the composition of pTyr and pSer/Thr peptides identified in the phosphoproteomic analysis. d Venn diagram showing overlap of phosphopeptides identified in MDA-MB-231 and 82T cells. e, f Gene ontology analysis of phosphoproteins in cancer epithelium and CAFs. e Cellular component; f molecular functions

Fig. 4

Reciprocal activation of receptor tyrosine kinases induced by the crosstalk. a Distribution of phosphorylation ratio of pY peptides. Blue dots: log₂-transformed ratio of MDA-MB-231-co-cultured versus MDA-MB-231; red dots: log₂-transformed ratio of 82T-co-cultured versus 82T. b, c Representative spectrum of FGFR1 (b) and EGFR (c) identified in cancer epithelium and CAFs. Top panels: MS spectra and bottom panels: MS/MS spectra for phosphotyrosine-containing peptides identified for FGFR1 and EGFR