Fig. 3: Effect of relative distance and orientation of the S/T-P sites from the D-motif on the c-JUN TAD N-terminal progressive multisite phosphorylation. | Nature Communications

Fig. 3: Effect of relative distance and orientation of the S/T-P sites from the D-motif on the c-JUN TAD N-terminal progressive multisite phosphorylation.

From: An intrinsic temporal order of c-JUN N-terminal phosphorylation regulates its activity by orchestrating co-factor recruitment

Fig. 3

a, b Schematic representation of the c-JUN TAD constructs S63A, S73A, T91A and T93A (a), and mDock and cDock (b) comparing to wild-type (WT). The initial rate of phosphorylation of residues by JNK1, determined by time-resolved NMR spectroscopy, is indicated according to the displayed colour scale. c, d Site-specific build-up curves of the phosphorylation of c-JUN mDock (c) and cDock (d) variants by JNK1, showing the mean of two biologically independent samples and fitted to single exponential build-up curves; pale lines show fits of wild-type c-JUN TAD (Fig. 1c) for comparison. Source data are provided as a Source Data file. e Crystal structure of JNK1 (grey surface) bound to a D-motif peptide (dark blue), superimposed with a crystal structure of a consensus T-P substrate peptide (magenta) bound to the homologous DYRK kinase (not shown). Arrows indicate the orientation of the bound peptides, with a hypothetical linker sequence indicated (dashed cyan). f Schematic representation summarizing the effect of the relative distance and orientation of the c-JUN TAD S/T-P residues from the D-motif on the temporal dynamics of the c-JUN N-terminal phosphorylation.

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