p53 de-ubiquitination: at the edge between life and death

被引：0
|
作者：
Paolo Salomoni
Pier Paolo Pandolfi
机构：
[1] Sloan-Kettering Institute,Molecular Biology Program and Department of Pathology
[2] Memorial Sloan-Kettering Cancer Center,undefined
来源：
Nature Cell Biology | 2002年 / 4卷
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摘要：
The tumour suppressor protein p53 is stabilized by the de-ubiquitination enzyme herpes-virus-associated ubiquitin-specific protease (HAUSP), which localizes to the promyelocytic leukaemia nuclear body (PML-NB). The pro-apoptotic activity of p53 is also induced by HAUSP. Therefore, p53 ubiquitination is a dynamic process, and HAUSP might function as a tumour suppressor by enhancing p53 stabilization.
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页码：E152 / E153
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