Skip to main content
. 2008 Oct 24;105(44):16958–16963. doi: 10.1073/pnas.0804608105

Fig. 5.

Fig. 5.

A proposed model for the regulation of p53 nuclear export by Thr-55 phosphorylation. In the absence of MDM2, Thr-55 phosphorylation enhances the p53-CRM1 interaction, which leads to nuclear export of p53 in MDM2-null cells. In the presence of MDM2, however, Thr-55 phosphorylation affects the p53-MDM2 interaction, resulting in monoubiquitination of p53, which unmasks p53 NES and promotes CRM1 binding.