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Letter
Nature Cell Biology 6, 665–672 (1 July 2004) | doi:10.1038/ncb1147
PML regulates p53 stability by sequestering Mdm2 to the nucleolus
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Abstract
The promyelocytic leukaemia (PML) tumour-suppressor protein potentiates p53 function by regulating post-translational modifications, such as CBP-dependent acetylation and Chk2-dependent phosphorylation, in the PML-Nuclear Body (NB). PML was recently shown to interact with the p53 ubiquitin-ligase Mdm2 (refs 4–6); however, the mechanism by which PML regulates Mdm2 remains unclear.
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