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      Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53

      , ,
      FEBS Letters
      Elsevier BV

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          Abstract

          The tumor suppressor p53 is degraded by the ubiquitin-proteasome system. p53 was polyubiquitinated in the presence of E1, UbcH5 as E2 and MDM2 oncoprotein. A ubiquitin molecule bound MDM2 through sulfhydroxy bond which is characteristic of ubiquitin ligase (E3)-ubiquitin binding. The cysteine residue in the carboxyl terminus of MDM2 was essential for the activity. These data suggest that the MDM2 protein, which is induced by p53, functions as a ubiquitin ligase, E3, in human papillomavirus-uninfected cells which do not have E6 protein.

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          The mdm-2 gene is induced in response to UV light in a p53-dependent manner.

          Irradiation of mammalian cells with UV light results in a dose-dependent accumulation of the p53 tumor-suppressor gene product that is evident within 2 hr. UV treatment causes a dramatic increase in p53-specific transcriptional transactivation activity and an increase in expression of the p53-responsive gene mdm-2. UV-stimulated mdm-2 expression is not directly correlated with the level of p53 protein in a cell because mdm-2 induction is delayed at high UV doses even though p53 levels rise almost immediately. Cells lacking p53 protein do not respond to UV by increasing their expression of mdm-2. The delayed induction of mdm-2 at high UV doses suggests that, in addition to p53 protein levels, other factors contribute to the regulation of mdm-2 expression following UV treatment. The time of induction of mdm-2 in cells treated with UV light correlates with recovery of normal rates of DNA synthesis, presumably after DNA repair. These data indicate a possible role for mdm-2 in cell cycle progression.
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            Author and article information

            Journal
            FEBS Letters
            Elsevier BV
            00145793
            December 22 1997
            December 22 1997
            January 20 1998
            : 420
            : 1
            : 25-27
            Article
            10.1016/S0014-5793(97)01480-4
            9450543
            9b48f1f9-216c-4ce9-a185-0f6b20ae07a9
            © 1998

            http://doi.wiley.com/10.1002/tdm_license_1.1

            http://onlinelibrary.wiley.com/termsAndConditions#vor

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