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
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Publicado: Nature Portfolio 2020
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Acceso en línea:https://doaj.org/article/80e8bf383dda460bb88d16b6b1cd6555
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spelling oai:doaj.org-article:80e8bf383dda460bb88d16b6b1cd65552021-12-02T15:33:33ZStructural basis for DNA damage-induced phosphoregulation of MDM2 RING domain10.1038/s41467-020-15783-y2041-1723https://doaj.org/article/80e8bf383dda460bb88d16b6b1cd65552020-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-15783-yhttps://doaj.org/toc/2041-1723p53 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.Helge M. MagnussenSyed F. AhmedGary. J. SibbetVentzislava A. HristovaKoji NomuraAndreas K. HockLewis J. ArchibaldAndrew G. JamiesonDavid FushmanKaren H. VousdenAllan M. WeissmanDanny T. HuangNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-15 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
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
Structural basis for DNA damage-induced phosphoregulation of MDM2 RING domain
description 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.
format article
author 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
author_facet 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
author_sort Helge M. Magnussen
title Structural basis for DNA damage-induced phosphoregulation of MDM2 RING domain
title_short Structural basis for DNA damage-induced phosphoregulation of MDM2 RING domain
title_full Structural basis for DNA damage-induced phosphoregulation of MDM2 RING domain
title_fullStr Structural basis for DNA damage-induced phosphoregulation of MDM2 RING domain
title_full_unstemmed Structural basis for DNA damage-induced phosphoregulation of MDM2 RING domain
title_sort structural basis for dna damage-induced phosphoregulation of mdm2 ring domain
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/80e8bf383dda460bb88d16b6b1cd6555
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