A dynamic role of HAUSP in the p53-Mdm2 pathway.

By Muyang Li, C. Brooks, N. Kon, W. Gu. Molecules and Cells, 2004

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The complexity of p53 stabilization and activation (2006, background): “Such an enzyme, HAUSP was identified by mass spectrometry as a p53-associated factor.(81) HAUSP stabilized p53 causing growth repression and apoptosis.”
A genomic and functional inventory of deubiquitinating enzymes. (2005, neutral): “In mammals, USP7 associates with HDM2, an E3 ligase critical for regulating p53 turnover, and thereby inhibits degradation of both HDM2 and p53 (Cummins et al., 2004; Li et al., 2004).”
RING domain E3 ubiquitin ligases. (2009, background): “Indeed, a deubiquitinating enzyme that binds and deubiquitinates Mdm2, Hausp, plays an important role in the Mdm2-p53 circuitry (146, 147).”
USP10 Regulates p53 Localization and Stability by Deubiquitinating p53 (2010, positive): “However, depletion of HAUSP in cells does not decrease p53 levels as predicted, but rather increases p53 levels (Cummins et al., 2004), apparently because of HAUSP's ability to bind and deubiquitinate Mdm2 (Cummins et al., 2004; Li et al., 2004).”
p53 ubiquitination: Mdm2 and beyond. (2006, background): “This simple linear model was obscured, however, with the finding that transient siRNA-mediated reduction or complete removal of HAUSP by somatic knockout in HCT116 cells led to profound p53 stability, observations that contradicted the proposed role of HAUSP in p53 stabilization (Cummins et al., 200”