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Article: MDM2 and MDMX bind and stabilize the p53-related protein p73

TitleMDM2 and MDMX bind and stabilize the p53-related protein p73
Authors
Issue Date1999
PublisherCell Press. The Journal's web site is located at http://www.current-biology.com/
Citation
Current Biology, 1999, v. 9 n. 15, p. 829-832 How to Cite?
AbstractThe p53 gene encodes one of the most important tumor suppressors in human cells and undergoes frequent mutational inactivation in cancers. MDM2, a transcriptional target of p53, binds p53 and can both inhibit p53-mediated transcription [1] [2] and target p53 for proteasome-mediated proteolysis [3] [4]. A close relative of p53, p73, has recently been identified [5] [6]. Here, we report that, like p53, p73alpha and the alternative transcription product p73beta also bind MDM2. Interaction between MDM2 and p53 represents a key step in the regulation of p53, as MDM2 promotes the degradation of p53. In striking contrast to p53, the half-life of p73 was found to be increased by binding to MDM2. Like MDM2, the MDM2-related protein MDMX also bound p73 and stabilized the level of p73. Moreover, the growth suppression functions of p73 and the induction of endogenous p21, a major mediator of the p53-dependent growth arrest pathway, were enhanced in the presence of MDM2. These differences between the regulation of p53 and p73 by MDM2/MDMX may highlight a physiological difference in their action.
Persistent Identifierhttp://hdl.handle.net/10722/194590
ISSN
2015 Impact Factor: 8.983
2015 SCImago Journal Rankings: 4.729
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorOngkeko, WM-
dc.contributor.authorWang, X-
dc.contributor.authorSiu, WY-
dc.contributor.authorLau, AWS-
dc.contributor.authorYamashita, K-
dc.contributor.authorHarris, AL-
dc.contributor.authorCox, LS-
dc.contributor.authorPoon, RYC-
dc.date.accessioned2014-02-13T04:19:12Z-
dc.date.available2014-02-13T04:19:12Z-
dc.date.issued1999-
dc.identifier.citationCurrent Biology, 1999, v. 9 n. 15, p. 829-832-
dc.identifier.issn0960-9822-
dc.identifier.urihttp://hdl.handle.net/10722/194590-
dc.description.abstractThe p53 gene encodes one of the most important tumor suppressors in human cells and undergoes frequent mutational inactivation in cancers. MDM2, a transcriptional target of p53, binds p53 and can both inhibit p53-mediated transcription [1] [2] and target p53 for proteasome-mediated proteolysis [3] [4]. A close relative of p53, p73, has recently been identified [5] [6]. Here, we report that, like p53, p73alpha and the alternative transcription product p73beta also bind MDM2. Interaction between MDM2 and p53 represents a key step in the regulation of p53, as MDM2 promotes the degradation of p53. In striking contrast to p53, the half-life of p73 was found to be increased by binding to MDM2. Like MDM2, the MDM2-related protein MDMX also bound p73 and stabilized the level of p73. Moreover, the growth suppression functions of p73 and the induction of endogenous p21, a major mediator of the p53-dependent growth arrest pathway, were enhanced in the presence of MDM2. These differences between the regulation of p53 and p73 by MDM2/MDMX may highlight a physiological difference in their action.-
dc.languageeng-
dc.publisherCell Press. The Journal's web site is located at http://www.current-biology.com/-
dc.relation.ispartofCurrent Biology-
dc.subject.meshDNA-Binding Proteins - genetics - metabolism-
dc.subject.meshNuclear Proteins - genetics - metabolism-
dc.subject.meshProto-Oncogene Proteins - genetics - metabolism-
dc.subject.meshRecombinant Fusion Proteins - genetics - metabolism-
dc.subject.meshTumor Suppressor Protein p53 - metabolism-
dc.titleMDM2 and MDMX bind and stabilize the p53-related protein p73en_US
dc.typeArticleen_US
dc.identifier.emailWang, X: xqwang@hkucc.hku.hk-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1016/S0960-9822(99)80367-4-
dc.identifier.pmid10469568-
dc.identifier.scopuseid_2-s2.0-0033615084-
dc.identifier.volume9-
dc.identifier.issue15-
dc.identifier.spage829-
dc.identifier.epage832-
dc.identifier.isiWOS:000081850800024-
dc.publisher.placeUnited States-

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