Editor's Summary

9 October 2008

PTEN ubiquitinylation in cancer

The exclusion of the tumour suppressor PTEN from the cell nucleus has been linked with tumour progression; the mechanisms behind its aberrant localization are obscure, although ubiquitinylation of specific lysines in PTEN is known to regulate PTEN distribution between the cytoplasm and nucleus. Now Min Sup Song identify HAUSP, a deubiquitinating enzyme previously shown to act on the p53 tumour repressor, as the enzyme responsible for PTEN deubiquitination too. This activity is shown to regulate the cellular localization and function of PTEN. This role of HAUSP is antagonized by PML, another tumour suppressor. PML function is disrupted in promeyelocytic leukaemia, and drugs that are effective in treating this form of leukaemia are found to impinge on PTEN function, by affecting PML and HAUSP.

LetterThe deubiquitinylation and localization of PTEN are regulated by a HAUSP–PML network

Min Sup Song, Leonardo Salmena, Arkaitz Carracedo, Ainara Egia, Francesco Lo-Coco, Julie Teruya-Feldstein & Pier Paolo Pandolfi