A tri-ionic anchor mechanism drives Ube2N-specific recruitment and K63-chain ubiquitination in TRIM ligases

The E3 ligase TRIM21 targets a broad range of pathogenic proteins using a unique mechanism. Here, the authors combine structural, biochemical and cell biological approaches to elucidate how TRIM21 selectively recruits its canonical E2 partner enzyme Ube2N and catalyzes ubiquitination.

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Autores principales:	Leo Kiss, Jingwei Zeng, Claire F. Dickson, Donna L. Mallery, Ji-Chun Yang, Stephen H. McLaughlin, Andreas Boland, David Neuhaus, Leo C. James
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/470293ee22be4d32ba89b9430667e524
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spelling	oai:doaj.org-article:470293ee22be4d32ba89b9430667e5242021-12-02T15:35:58ZA tri-ionic anchor mechanism drives Ube2N-specific recruitment and K63-chain ubiquitination in TRIM ligases10.1038/s41467-019-12388-y2041-1723https://doaj.org/article/470293ee22be4d32ba89b9430667e5242019-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-12388-yhttps://doaj.org/toc/2041-1723The E3 ligase TRIM21 targets a broad range of pathogenic proteins using a unique mechanism. Here, the authors combine structural, biochemical and cell biological approaches to elucidate how TRIM21 selectively recruits its canonical E2 partner enzyme Ube2N and catalyzes ubiquitination.Leo KissJingwei ZengClaire F. DicksonDonna L. MalleryJi-Chun YangStephen H. McLaughlinAndreas BolandDavid NeuhausLeo C. JamesNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-13 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Leo Kiss Jingwei Zeng Claire F. Dickson Donna L. Mallery Ji-Chun Yang Stephen H. McLaughlin Andreas Boland David Neuhaus Leo C. James A tri-ionic anchor mechanism drives Ube2N-specific recruitment and K63-chain ubiquitination in TRIM ligases
description	The E3 ligase TRIM21 targets a broad range of pathogenic proteins using a unique mechanism. Here, the authors combine structural, biochemical and cell biological approaches to elucidate how TRIM21 selectively recruits its canonical E2 partner enzyme Ube2N and catalyzes ubiquitination.
format	article
author	Leo Kiss Jingwei Zeng Claire F. Dickson Donna L. Mallery Ji-Chun Yang Stephen H. McLaughlin Andreas Boland David Neuhaus Leo C. James
author_facet	Leo Kiss Jingwei Zeng Claire F. Dickson Donna L. Mallery Ji-Chun Yang Stephen H. McLaughlin Andreas Boland David Neuhaus Leo C. James
author_sort	Leo Kiss
title	A tri-ionic anchor mechanism drives Ube2N-specific recruitment and K63-chain ubiquitination in TRIM ligases
title_short	A tri-ionic anchor mechanism drives Ube2N-specific recruitment and K63-chain ubiquitination in TRIM ligases
title_full	A tri-ionic anchor mechanism drives Ube2N-specific recruitment and K63-chain ubiquitination in TRIM ligases
title_fullStr	A tri-ionic anchor mechanism drives Ube2N-specific recruitment and K63-chain ubiquitination in TRIM ligases
title_full_unstemmed	A tri-ionic anchor mechanism drives Ube2N-specific recruitment and K63-chain ubiquitination in TRIM ligases
title_sort	tri-ionic anchor mechanism drives ube2n-specific recruitment and k63-chain ubiquitination in trim ligases
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/470293ee22be4d32ba89b9430667e524
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A tri-ionic anchor mechanism drives Ube2N-specific recruitment and K63-chain ubiquitination in TRIM ligases

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