Structural basis for DNA damage-induced phosphoregulation of MDM2 RING domain

p53 is an important tumor suppressor protein which is regulated by the E3 ubiquitin ligase MDM2. Here the authors reveal that DNA damage-induced Ser429 phosphorylation of MDM2 serve to boost the activity of MDM2 homodimer by stabilizing the active E2–ubiquitin complex and promote its self-destructio...

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Autores principales: Helge M. Magnussen, Syed F. Ahmed, Gary. J. Sibbet, Ventzislava A. Hristova, Koji Nomura, Andreas K. Hock, Lewis J. Archibald, Andrew G. Jamieson, David Fushman, Karen H. Vousden, Allan M. Weissman, Danny T. Huang
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/80e8bf383dda460bb88d16b6b1cd6555
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Sumario:p53 is an important tumor suppressor protein which is regulated by the E3 ubiquitin ligase MDM2. Here the authors reveal that DNA damage-induced Ser429 phosphorylation of MDM2 serve to boost the activity of MDM2 homodimer by stabilizing the active E2–ubiquitin complex and promote its self-destruction to enable rapid p53 stabilization.