Fig. 5: RanBP2 is necessary for the TSPYL5/G3BP1-mediated p53 sumoylation. | Cell Death & Disease

Fig. 5: RanBP2 is necessary for the TSPYL5/G3BP1-mediated p53 sumoylation.

From: TSPYL5-driven G3BP1 nuclear membrane translocation facilitates p53 cytoplasm sequestration via accelerating RanBP2-mediated p53 sumoylation and nuclear export in neuroblastoma

Fig. 5

A Mass spectrometry analysis identified RanBP2 in the binding protein pool of G3BP1. B Endogenous interaction between G3BP1 and RanBP2 was determined using Co-IP with anti-G3BP1 antibodies in SK-N-SH cells. C The binding sites of G3BP1 and RanBP2 proposed by computational docking model. G3BP1 molecule was shown as blue sticks, and RanBP2 was shown as pink sticks. D Interaction between the PXXP domain of G3BP1 and RanBP2 was determined using Co-IP with anti-HA antibodies. The G1 to G4 domains of G3BP1 are same to that in Fig. 6D. E Two-step Co-IP assays showed the present of RanBP2-G3BP1-p53 complex in SK-N-SH cells. F G3BP1 overexpression increased the binding of p53 to RanBP2 in SK-N-SH cells using IP with anti-RanBP2 antibodies. Data are presented as the mean ± SD from 3 experiments, ***p < 0.001. G Immunofluorescence analysis showed the nuclear import of p53 in SK-N-SH cells with RanBP2 knockdown. Scale bar = 20 μm.

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