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Dynamic changes of protein phosphorylation identify ERK1/2 substrates from cytosolic and nuclear compartments. Dynamic changes of protein phosphorylation.

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Presentation on theme: "Dynamic changes of protein phosphorylation identify ERK1/2 substrates from cytosolic and nuclear compartments. Dynamic changes of protein phosphorylation."— Presentation transcript:

1 Dynamic changes of protein phosphorylation identify ERK1/2 substrates from cytosolic and nuclear compartments. Dynamic changes of protein phosphorylation identify ERK1/2 substrates from cytosolic and nuclear compartments. (A) Two‐dimensional representation of quantitative changes in protein phosphorylation following serum stimulation and PD treatment. Each point corresponds to a different phosphopeptide. Candidate ERK1/2 substrates are shown as dark blue circles in the bottom right quadrant and represent phosphopeptides displaying increase in phosphorylation upon serum stimulation and decrease upon PD treatment (two‐tailed t‐test). Note that a few peptides with (pS/T)‐P sites in this quadrant did not have significant abundance change and were not retained as ERK1/2 candidates. Yellow circles correspond to previously known ERK1/2 substrates. (B, C) GO analysis. Candidate ERK1/2 substrates were annotated and classified according to (B) biological process or (C) cellular component GO terms. P is the P‐value of Fisher's exact test and E is the calculated odds ratio for category enrichment. Only E‐values above 1 are presented. A subset of proteins belonging to each category is shown. Substrates validated by in vitro kinase assays are shown in red. Mathieu Courcelles et al. Mol Syst Biol 2013;9:669 © as stated in the article, figure or figure legend


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