title: Limiting the power of p53 through the ubiquitin proteasome pathway.
abstract: The ubiquitin proteasome pathway is critical in restraining the activities of the p53 tumor suppressor. Numerous E3 and E4 ligases regulate p53 levels. Additionally, deubquitinating enzymes that modify p53 directly or indirectly also impact p53 function. When alterations of these proteins result in increased p53 activity, cells arrest in the cell cycle, senesce, or apoptose. On the other hand, alterations that result in decreased p53 levels yield tumor-prone phenotypes. This review focuses on the physiological relevance of these important regulators of p53 and their therapeutic implications.
authors.affiliation: Department of Genetics, The University of Texas M.D. Anderson Cancer Center, Houston, Texas 77030, USA.
authors.forename: Vinod
authors.initials: V
authors.lastname: Pant
authors.affiliation: Department of Genetics, The University of Texas M.D. Anderson Cancer Center, Houston, Texas 77030, USA gglozano@mdanderson.org.
authors.forename: Guillermina
authors.initials: G
authors.lastname: Lozano
mesh_terms: D000818:Animals; D006801:Humans; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism*; D055550:Protein Stability; D051736:Proto-Oncogene Proteins c-mdm2 / Q000378:metabolism; D016159:Tumor Suppressor Protein p53 / Q000235:genetics / Q000378:metabolism*; D025801:Ubiquitin / Q000378:metabolism*; D054875:Ubiquitination
chemical_list: D016159:Tumor Suppressor Protein p53; D025801:Ubiquitin; D051736:Proto-Oncogene Proteins c-mdm2; D046988:Proteasome Endopeptidase Complex
keywords: Mdm2; mouse models; p53 regulation; ubiquitination