Fig. 6: pY445 alters the structure and function of the PBD. | Nature Communications

Fig. 6: pY445 alters the structure and function of the PBD.

From: The Eyes Absent family members EYA4 and EYA1 promote PLK1 activation and successful mitosis through tyrosine dephosphorylation

Fig. 6

A Co-immunoprecipitation reactions with overexpressed PLK1-myc WT or PLK1-myc Y445F in RO3306 arrested G2 cells and nocodazole arrested M-phase cells. Western blots from protein lysates (left panel), and western blots from G2 arrested eluates (middle panel) and M-phase arrested cells (right panel). B Representative simulation snapshot of the backside of the phosphopeptide binding pocket of PLK1s PBD (bound phosphopeptide in yellow). Y445 is indicated in a phosphorylated state (pY445). The image highlights the interaction of pY445 with R507 (green sticks), as well as hydrogen bonds formed by D429 and N446, and increased rigidity within the connecting loop (AA 502-506) highlighted in orange. C, D Plots of the root mean square fluctuation (RMSF) of Cα atoms in the WT PLK1 PBD (black line) and Y445-phosphorylated PLK1 PBD (red line). The decreased RMSF within the connecting loop (AA 502-506) is indicative of decreased flexibility either when the PBD is bound to a model phosphopeptide (C), or in the unbound state (D) (n = 5 simulations). Source data are provided as a Source data file.

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