Proteasomal degradation of the tumour suppressor FBW7 requires branched ubiquitylation by TRIP12

The tumor suppressor FBW7 is a substrate adaptor for the E3 ubiquitin ligase complex SKP1-CUL1-F-box (SCF) and itself a target for ubiquitylation. Here, the authors show that TRIP12 mediates branched K11-linked ubiquitylation of FBW7, to regulate its stability and thus abundance of a subset of SCFFB...

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Autores principales:	Omar M. Khan, Jorge Almagro, Jessica K. Nelson, Stuart Horswell, Vesela Encheva, Kripa S. Keyan, Bruce E. Clurman, Ambrosius P. Snijders, Axel Behrens
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/6e27448b8929476da30da600acc41eb2
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spelling	oai:doaj.org-article:6e27448b8929476da30da600acc41eb22021-12-02T18:15:35ZProteasomal degradation of the tumour suppressor FBW7 requires branched ubiquitylation by TRIP1210.1038/s41467-021-22319-52041-1723https://doaj.org/article/6e27448b8929476da30da600acc41eb22021-04-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-22319-5https://doaj.org/toc/2041-1723The tumor suppressor FBW7 is a substrate adaptor for the E3 ubiquitin ligase complex SKP1-CUL1-F-box (SCF) and itself a target for ubiquitylation. Here, the authors show that TRIP12 mediates branched K11-linked ubiquitylation of FBW7, to regulate its stability and thus abundance of a subset of SCFFBW7 substrates.Omar M. KhanJorge AlmagroJessica K. NelsonStuart HorswellVesela EnchevaKripa S. KeyanBruce E. ClurmanAmbrosius P. SnijdersAxel BehrensNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-14 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Omar M. Khan Jorge Almagro Jessica K. Nelson Stuart Horswell Vesela Encheva Kripa S. Keyan Bruce E. Clurman Ambrosius P. Snijders Axel Behrens Proteasomal degradation of the tumour suppressor FBW7 requires branched ubiquitylation by TRIP12
description	The tumor suppressor FBW7 is a substrate adaptor for the E3 ubiquitin ligase complex SKP1-CUL1-F-box (SCF) and itself a target for ubiquitylation. Here, the authors show that TRIP12 mediates branched K11-linked ubiquitylation of FBW7, to regulate its stability and thus abundance of a subset of SCFFBW7 substrates.
format	article
author	Omar M. Khan Jorge Almagro Jessica K. Nelson Stuart Horswell Vesela Encheva Kripa S. Keyan Bruce E. Clurman Ambrosius P. Snijders Axel Behrens
author_facet	Omar M. Khan Jorge Almagro Jessica K. Nelson Stuart Horswell Vesela Encheva Kripa S. Keyan Bruce E. Clurman Ambrosius P. Snijders Axel Behrens
author_sort	Omar M. Khan
title	Proteasomal degradation of the tumour suppressor FBW7 requires branched ubiquitylation by TRIP12
title_short	Proteasomal degradation of the tumour suppressor FBW7 requires branched ubiquitylation by TRIP12
title_full	Proteasomal degradation of the tumour suppressor FBW7 requires branched ubiquitylation by TRIP12
title_fullStr	Proteasomal degradation of the tumour suppressor FBW7 requires branched ubiquitylation by TRIP12
title_full_unstemmed	Proteasomal degradation of the tumour suppressor FBW7 requires branched ubiquitylation by TRIP12
title_sort	proteasomal degradation of the tumour suppressor fbw7 requires branched ubiquitylation by trip12
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/6e27448b8929476da30da600acc41eb2
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Proteasomal degradation of the tumour suppressor FBW7 requires branched ubiquitylation by TRIP12

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