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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Main Authors:	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
Format:	article
Language:	EN
Published:	Nature Portfolio 2020
Subjects:	Science Q
Online Access:	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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Structural basis for DNA damage-induced phosphoregulation of MDM2 RING domain

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