A quaternary tetramer assembly inhibits the deubiquitinating activity of USP25
USP25 is a deubiquitinating enzyme and a positive regulator of Wnt/β-catenin signaling. Here the authors present the crystal structure of USP25 in a tetrameric inactive state and their biochemical and kinetic assays support an USP25 autoinhibitory mechanism that is mediated through a dimer to tetram...
Guardado en:
Autores principales: | , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
|
Materias: | |
Acceso en línea: | https://doaj.org/article/d3952516fdd9440481efad6314284dfd |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:d3952516fdd9440481efad6314284dfd |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:d3952516fdd9440481efad6314284dfd2021-12-02T14:41:17ZA quaternary tetramer assembly inhibits the deubiquitinating activity of USP2510.1038/s41467-018-07510-52041-1723https://doaj.org/article/d3952516fdd9440481efad6314284dfd2018-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-07510-5https://doaj.org/toc/2041-1723USP25 is a deubiquitinating enzyme and a positive regulator of Wnt/β-catenin signaling. Here the authors present the crystal structure of USP25 in a tetrameric inactive state and their biochemical and kinetic assays support an USP25 autoinhibitory mechanism that is mediated through a dimer to tetramerization transition.Bing LiuMarta Sureda-GómezYang ZhenVirginia AmadorDavid ReverterNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-13 (2018) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
Science Q |
spellingShingle |
Science Q Bing Liu Marta Sureda-Gómez Yang Zhen Virginia Amador David Reverter A quaternary tetramer assembly inhibits the deubiquitinating activity of USP25 |
description |
USP25 is a deubiquitinating enzyme and a positive regulator of Wnt/β-catenin signaling. Here the authors present the crystal structure of USP25 in a tetrameric inactive state and their biochemical and kinetic assays support an USP25 autoinhibitory mechanism that is mediated through a dimer to tetramerization transition. |
format |
article |
author |
Bing Liu Marta Sureda-Gómez Yang Zhen Virginia Amador David Reverter |
author_facet |
Bing Liu Marta Sureda-Gómez Yang Zhen Virginia Amador David Reverter |
author_sort |
Bing Liu |
title |
A quaternary tetramer assembly inhibits the deubiquitinating activity of USP25 |
title_short |
A quaternary tetramer assembly inhibits the deubiquitinating activity of USP25 |
title_full |
A quaternary tetramer assembly inhibits the deubiquitinating activity of USP25 |
title_fullStr |
A quaternary tetramer assembly inhibits the deubiquitinating activity of USP25 |
title_full_unstemmed |
A quaternary tetramer assembly inhibits the deubiquitinating activity of USP25 |
title_sort |
quaternary tetramer assembly inhibits the deubiquitinating activity of usp25 |
publisher |
Nature Portfolio |
publishDate |
2018 |
url |
https://doaj.org/article/d3952516fdd9440481efad6314284dfd |
work_keys_str_mv |
AT bingliu aquaternarytetramerassemblyinhibitsthedeubiquitinatingactivityofusp25 AT martasuredagomez aquaternarytetramerassemblyinhibitsthedeubiquitinatingactivityofusp25 AT yangzhen aquaternarytetramerassemblyinhibitsthedeubiquitinatingactivityofusp25 AT virginiaamador aquaternarytetramerassemblyinhibitsthedeubiquitinatingactivityofusp25 AT davidreverter aquaternarytetramerassemblyinhibitsthedeubiquitinatingactivityofusp25 AT bingliu quaternarytetramerassemblyinhibitsthedeubiquitinatingactivityofusp25 AT martasuredagomez quaternarytetramerassemblyinhibitsthedeubiquitinatingactivityofusp25 AT yangzhen quaternarytetramerassemblyinhibitsthedeubiquitinatingactivityofusp25 AT virginiaamador quaternarytetramerassemblyinhibitsthedeubiquitinatingactivityofusp25 AT davidreverter quaternarytetramerassemblyinhibitsthedeubiquitinatingactivityofusp25 |
_version_ |
1718389961265250304 |