Phosphorylation levels of JAK2 after addition of increasing Epo-concentrations: model approach (Figure 5a)

The present dataset contain source data for Figure 5a from Schilling et al., 2009. Cell fate decisions are regulated by the coordinated activation of signalling pathways such as the extracellular signal-regulated kinase (ERK) cascade, but contributions of individual kinase isoforms are mostly unknown. The authors combined quantitative data from erythropoietin-induced pathway activation in primary erythroid progenitor (colony-forming unit erythroid stage, CFU-E) cells with mathematical modelling, in order to predict and experimentally confirmed a distributive ERK phosphorylation mechanism in CFU-E cells. The authors found evidences that double-phosphorylated ERK1 attenuates proliferation beyond a certain activation level, whereas activated ERK2 enhances proliferation with saturation kinetics. Phosphorylation levels of JAK2 at 7 min after stimulation for Epo concentrations ranging from 0.1 to 1000 U/ml were simulated.