HAUSP (also known as deubiquitinating enzyme 7, herpes virus associated ubiquitin specific protease, TEF1, ubiquitin carboxyl terminal hydrolase 7, ubiquitin specific protease 7, ubiquitin thiolesterase 7, and USP7) is a novel p53 interacting protein. HAUSP was identified by mass spectrometry of affinity purified p53 associated factors by Li et al. HAUSP strongly stabilizes p53, even in the presence of excess MDM2, and also induces p53-dependent cell growth repression and apoptosis. HAUSP has an intrinsic enzymatic activity that specifically de-ubiquitinates p53 both in vivo and in vitro. Expression of a catalytically inactive point mutation of HAUSP in cells increased the levels of p53 ubiquitination and also destabilized p53. Li et al concluded that their findings revealed an important mechanism by which p53 can be stabilized by direct de-ubiquitination and also implied that HAUSP may function as a tumor suppressor in vivo through the stabilization of p53.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.