title: p53 ubiquitination: Mdm2 and beyond.
abstract: Although early studies have suggested that the oncoprotein Mdm2 is the primary E3 ubiquitin ligase for the p53 tumor suppressor, an increasing amount of data suggests that p53 ubiquitination and degradation are more complex than once thought. The discoveries of MdmX, HAUSP, ARF, COP1, Pirh2, and ARF-BP1 continue to uncover the multiple facets of this pathway. There is no question that Mdm2 plays a pivotal role in downregulating p53 activities in numerous cellular settings. Nevertheless, growing evidence challenges the conventional view that Mdm2 is essential for p53 turnover.
authors.affiliation: Institute for Cancer Genetics and Department of Pathology, College of Physicians and Surgeons, Columbia University, 1150 St. Nicholas Avenue, New York, New York 10032, USA.
authors.forename: Christopher L
authors.initials: CL
authors.lastname: Brooks
authors.forename: Wei
authors.initials: W
authors.lastname: Gu
mesh_terms: D000818:Animals; D002460:Cell Line; D002470:Cell Survival; D019143:Evolution, Molecular; D006801:Humans; D051736:Proto-Oncogene Proteins c-mdm2 / Q000235:genetics / Q000378:metabolism*; D016159:Tumor Suppressor Protein p53 / Q000235:genetics / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases / Q000235:genetics / Q000378:metabolism
chemical_list: D016159:Tumor Suppressor Protein p53; D025801:Ubiquitin; D051736:Proto-Oncogene Proteins c-mdm2; D044767:Ubiquitin-Protein Ligases