UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins
The U-box ubiquitin ligase UFD-2 is one of the most abundant components of the ubiquitin proteasome system in muscle cells. Here the authors perform in vitro and in vivo experiments and show that UFD-2 has E3 ligase activity and that it ubiquitinates unfolded myosin using the C. elegans myosin chape...
Guardado en:
Autores principales: | , , , , , , , , |
---|---|
Formato: | article |
Lenguaje: | EN |
Publicado: |
Nature Portfolio
2018
|
Materias: | |
Acceso en línea: | https://doaj.org/article/5d615670363d4e18b6f7439c5d092bfd |
Etiquetas: |
Agregar Etiqueta
Sin Etiquetas, Sea el primero en etiquetar este registro!
|
id |
oai:doaj.org-article:5d615670363d4e18b6f7439c5d092bfd |
---|---|
record_format |
dspace |
spelling |
oai:doaj.org-article:5d615670363d4e18b6f7439c5d092bfd2021-12-02T15:33:37ZUFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins10.1038/s41467-018-02924-72041-1723https://doaj.org/article/5d615670363d4e18b6f7439c5d092bfd2018-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-02924-7https://doaj.org/toc/2041-1723The U-box ubiquitin ligase UFD-2 is one of the most abundant components of the ubiquitin proteasome system in muscle cells. Here the authors perform in vitro and in vivo experiments and show that UFD-2 has E3 ligase activity and that it ubiquitinates unfolded myosin using the C. elegans myosin chaperone UNC-45 as an adaptor protein.Doris HellerschmiedMax RoesslerAnita LehnerLinn GazdaKarel StejskalRichard ImreKarl MechtlerAlexander DammermannTim ClausenNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-15 (2018) |
institution |
DOAJ |
collection |
DOAJ |
language |
EN |
topic |
Science Q |
spellingShingle |
Science Q Doris Hellerschmied Max Roessler Anita Lehner Linn Gazda Karel Stejskal Richard Imre Karl Mechtler Alexander Dammermann Tim Clausen UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins |
description |
The U-box ubiquitin ligase UFD-2 is one of the most abundant components of the ubiquitin proteasome system in muscle cells. Here the authors perform in vitro and in vivo experiments and show that UFD-2 has E3 ligase activity and that it ubiquitinates unfolded myosin using the C. elegans myosin chaperone UNC-45 as an adaptor protein. |
format |
article |
author |
Doris Hellerschmied Max Roessler Anita Lehner Linn Gazda Karel Stejskal Richard Imre Karl Mechtler Alexander Dammermann Tim Clausen |
author_facet |
Doris Hellerschmied Max Roessler Anita Lehner Linn Gazda Karel Stejskal Richard Imre Karl Mechtler Alexander Dammermann Tim Clausen |
author_sort |
Doris Hellerschmied |
title |
UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins |
title_short |
UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins |
title_full |
UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins |
title_fullStr |
UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins |
title_full_unstemmed |
UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins |
title_sort |
ufd-2 is an adaptor-assisted e3 ligase targeting unfolded proteins |
publisher |
Nature Portfolio |
publishDate |
2018 |
url |
https://doaj.org/article/5d615670363d4e18b6f7439c5d092bfd |
work_keys_str_mv |
AT dorishellerschmied ufd2isanadaptorassistede3ligasetargetingunfoldedproteins AT maxroessler ufd2isanadaptorassistede3ligasetargetingunfoldedproteins AT anitalehner ufd2isanadaptorassistede3ligasetargetingunfoldedproteins AT linngazda ufd2isanadaptorassistede3ligasetargetingunfoldedproteins AT karelstejskal ufd2isanadaptorassistede3ligasetargetingunfoldedproteins AT richardimre ufd2isanadaptorassistede3ligasetargetingunfoldedproteins AT karlmechtler ufd2isanadaptorassistede3ligasetargetingunfoldedproteins AT alexanderdammermann ufd2isanadaptorassistede3ligasetargetingunfoldedproteins AT timclausen ufd2isanadaptorassistede3ligasetargetingunfoldedproteins |
_version_ |
1718387084964659200 |