Analysis of phosphoproteomic changes during N-starvation.

<p>Changes in the phosphoproteome of heterothallic cells in a time course of nitrogen starvation starting at t0 = plating of cells on MSL-N plates 2 h after transfer to liquid MSL-N. (<b>A</b>) Heatmap of the significant changes in 3,100 phosphosites during nitrogen starvation, showing 2 major clusters of sites whose phosphorylation increase (1) or decrease (2). Corresponding protein dynamics is shown on the right with missing values in gray. Regression analysis estimated that about 78% of phosphosite level changes are independent of the changes in protein levels (see <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3002963#pbio.3002963.g003" target="_blank">Fig 3C</a>). The underlying data can be found in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3002963#pbio.3002963.s008" target="_blank">S1 Table</a>. (<b>B</b>) Significant fold enrichment in GO annotations for biological processes, molecular functions, and cellular components of proteins containing one or several sites showing phosphorylation increase during nitrogen starvation. (<b>C</b>) Significant fold enrichment in GO annotations for biological processes, molecular functions, and cellular components of proteins containing one or several sites showing phosphorylation decrease during nitrogen starvation. Significance levels were assessed by Fisher’s exact test and corrected for false discovery rate.</p> <p>(PDF)</p>

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2024-12-20
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https://doi.org/10.1371/journal.pbio.3002963.s004
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Educational Robotics and Engineering
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Analysis of phosphoproteomic changes during N-starvation.

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Educational Robotics and Engineering
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Analysis of phosphoproteomic changes during N-starvation.

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Abstract

<p>Changes in the phosphoproteome of heterothallic cells in a time course of nitrogen starvation starting at t0 = plating of cells on MSL-N plates 2 h after transfer to liquid MSL-N. (<b>A</b>) Heatmap of the significant changes in 3,100 phosphosites during nitrogen starvation, showing 2 major clusters of sites whose phosphorylation increase (1) or decrease (2). Corresponding protein dynamics is shown on the right with missing values in gray. Regression analysis estimated that about 78% of phosphosite level changes are independent of the changes in protein levels (see <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3002963#pbio.3002963.g003" target="_blank">Fig 3C</a>). The underlying data can be found in <a href="http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.3002963#pbio.3002963.s008" target="_blank">S1 Table</a>. (<b>B</b>) Significant fold enrichment in GO annotations for biological processes, molecular functions, and cellular components of proteins containing one or several sites showing phosphorylation increase during nitrogen starvation. (<b>C</b>) Significant fold enrichment in GO annotations for biological processes, molecular functions, and cellular components of proteins containing one or several sites showing phosphorylation decrease during nitrogen starvation. Significance levels were assessed by Fisher’s exact test and corrected for false discovery rate.</p> <p>(PDF)</p>

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