Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism

Ubiquitin (Ub) receptors are responsible for the recognition of ubiquitylated proteins. Here the authors describe the crystal structure of the ubiquitylated form of the Ub-receptor Rpn10, which suggest that ubiquitylation of Rpn10 promotes its dissociation from the proteasome.

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Autores principales:	Tal Keren-Kaplan, Lee Zeev Peters, Olga Levin-Kravets, Ilan Attali, Oded Kleifeld, Noa Shohat, Shay Artzi, Ori Zucker, Inbar Pilzer, Noa Reis, Michael H. Glickman, Shay Ben-Aroya, Gali Prag
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/8431d5b994ec4a4ca5d12daa3a68d3a3
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spelling	oai:doaj.org-article:8431d5b994ec4a4ca5d12daa3a68d3a32021-12-02T14:39:14ZStructure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism10.1038/ncomms129602041-1723https://doaj.org/article/8431d5b994ec4a4ca5d12daa3a68d3a32016-10-01T00:00:00Zhttps://doi.org/10.1038/ncomms12960https://doaj.org/toc/2041-1723Ubiquitin (Ub) receptors are responsible for the recognition of ubiquitylated proteins. Here the authors describe the crystal structure of the ubiquitylated form of the Ub-receptor Rpn10, which suggest that ubiquitylation of Rpn10 promotes its dissociation from the proteasome.Tal Keren-KaplanLee Zeev PetersOlga Levin-KravetsIlan AttaliOded KleifeldNoa ShohatShay ArtziOri ZuckerInbar PilzerNoa ReisMichael H. GlickmanShay Ben-AroyaGali PragNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Tal Keren-Kaplan Lee Zeev Peters Olga Levin-Kravets Ilan Attali Oded Kleifeld Noa Shohat Shay Artzi Ori Zucker Inbar Pilzer Noa Reis Michael H. Glickman Shay Ben-Aroya Gali Prag Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism
description	Ubiquitin (Ub) receptors are responsible for the recognition of ubiquitylated proteins. Here the authors describe the crystal structure of the ubiquitylated form of the Ub-receptor Rpn10, which suggest that ubiquitylation of Rpn10 promotes its dissociation from the proteasome.
format	article
author	Tal Keren-Kaplan Lee Zeev Peters Olga Levin-Kravets Ilan Attali Oded Kleifeld Noa Shohat Shay Artzi Ori Zucker Inbar Pilzer Noa Reis Michael H. Glickman Shay Ben-Aroya Gali Prag
author_facet	Tal Keren-Kaplan Lee Zeev Peters Olga Levin-Kravets Ilan Attali Oded Kleifeld Noa Shohat Shay Artzi Ori Zucker Inbar Pilzer Noa Reis Michael H. Glickman Shay Ben-Aroya Gali Prag
author_sort	Tal Keren-Kaplan
title	Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism
title_short	Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism
title_full	Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism
title_fullStr	Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism
title_full_unstemmed	Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism
title_sort	structure of ubiquitylated-rpn10 provides insight into its autoregulation mechanism
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/8431d5b994ec4a4ca5d12daa3a68d3a3
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Structure of ubiquitylated-Rpn10 provides insight into its autoregulation mechanism

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