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Fig. 2 | Cancer & Metabolism

Fig. 2

From: Phosphoproteomics revealed cellular signals immediately responding to disruption of cancer amino acid homeostasis induced by inhibition of l-type amino acid transporter 1

Fig. 2

Phosphoproteomics of BTC cell lines subjected to short-time JPH203 treatment. A Quantitative phosphoproteomics workflow for studying the effects of short-time LAT1 inhibition on BTC cells. Tryptic peptide samples were prepared from cells treated with 30 μM JPH203 for 15 and 30 min, and the control non-treated cells (n = 3). Phosphopeptides were enriched by IMAC. After being labeled with TMT reagent and mixed, phosphopeptide samples were subject to high pH C18 fractionation. All fractions were analyzed by Q-Exactive mass spectrometer. B Representative scatter plots showing log2 fold changes of phosphoproteome between biological replicates of JPH203-treated/control samples of KKU-055 cells treated with JPH203 for 30 min. Plots of differentially phosphorylated sites are shown in red. C Representative phosphoproteomics data from JPH203-treated and control samples of KKU-055 cells treated with JPH203 for 30 min. A volcano plot was generated by plotting -log10 p values against log2 fold changes of relative abundance ratio between JPH203-treated/control samples. Plots of differentially phosphorylated sites are shown in green and blue. D The number of differentially phosphorylated sites in cells subjected to short-time LAT1 inhibition. The bars of upregulated and downregulated phosphorylation sites are shown in red and blue, respectively

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Cancer & Metabolism

ISSN: 2049-3002