Correction: Corrigendum

In our recent paper, Zhou, B. P. et al. Nature Cell Biology 3, 973–982 (2001), we reported incorrect references for mapping the p14^Arf binding site on MDM2. These references should have been Mol. Cell. Biol. 20, 2517–2528 (2000) and J. Mol. Biol. 314, 263–277 (2001). In these papers, the authors demonstrated that the p14^Arf binding site on MDM2 is found in residues 235–264 and 270–289.

In addition, our interpretation of the data on p19^ARF in Fig. 7a is incorrect. The NIH3T3 cell line used in Fig. 7a has bi-allelic deletion of the ARF/Ink4a locus (Oncogene 11, 635–64 (1995)). The antibody originally used in Fig. 7a recognizes p19^Ink4d, and not p19^ARF. To clarify these results, we repeated the experiments using the p19^ARF antibody in p19^ARF-expressing cells (mouse embryonic fibroblasts (MEFs) and DM3T3 cells; Oncogene, 11, 635–645 (1995)). The results shown in Fig. 1 indicate that blockage of phosphatidylinositol-3-OH kinase (PI(3)K/Akt activity with wortmannin enhanced the interaction of p19^ARF and MDM2. Thus, these results and the original results from Fig. 7c, support the conclusion that blockage of the PI(3)K/Akt pathway enhances the binding affinity between p19^ARF and MDM2. Although the Akt phosphorylation sites on MDM2 did not overlap with the binding region for p19^ARF (Ser 166, Ser 186 versus the regions of amino acids 235–264 and 270–289), phosphorylation of MDM2 by Akt in these sites may induce conformation changes and consequently affect the binding of p19^ARF.

Figure 1: Blockage of PI(3)K/Akt pathway enhances the binding of MDM2 and p19^ARF.

a, MEF and DM3T3 cells were incubated with or without 100 nM wortmannin for 5 h. Lysates were then immunoprecipitated with an anti-MDM2 antibody before western blotting for MDM2 and p19^ARF (R562; Abcam Inc., Cambridge, UK). b, MDM2 was transfected into p53^−/−, MDM2^−/− MEF cells and the cells were treated as in a. Lysates were immunoprecipitated and analysed by western blotting. c, Haemagglutinin (HA)-tagged p19^ARF was transfected into p19^ARF−/− MEF cells and the cells were treated as in a. Lysates were immunoprecipitated with an anti-HA anti-body before western blotting.