UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteins

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...

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Main Authors: Doris Hellerschmied, Max Roessler, Anita Lehner, Linn Gazda, Karel Stejskal, Richard Imre, Karl Mechtler, Alexander Dammermann, Tim Clausen
Format: Article
Language:English
Published: Nature Publishing Group 2018-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/s41467-018-02924-7
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spelling doaj-5d615670363d4e18b6f7439c5d092bfd2021-05-11T09:37:47ZengNature Publishing GroupNature Communications2041-17232018-02-019111510.1038/s41467-018-02924-7UFD-2 is an adaptor-assisted E3 ligase targeting unfolded proteinsDoris Hellerschmied0Max Roessler1Anita Lehner2Linn Gazda3Karel Stejskal4Richard Imre5Karl Mechtler6Alexander Dammermann7Tim Clausen8Research Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC)Max F. Perutz Laboratories (MFPL), University of ViennaVienna Biocenter Core Facilities, Doktor-Bohr-Gasse 3Research Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC)Research Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC)Research Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC)Research Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC)Max F. Perutz Laboratories (MFPL), University of ViennaResearch Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC)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.https://doi.org/10.1038/s41467-018-02924-7
collection DOAJ
language English
format Article
sources DOAJ
author Doris Hellerschmied
Max Roessler
Anita Lehner
Linn Gazda
Karel Stejskal
Richard Imre
Karl Mechtler
Alexander Dammermann
Tim Clausen
spellingShingle 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
Nature Communications
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 Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2018-02-01
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.
url https://doi.org/10.1038/s41467-018-02924-7
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AT maxroessler ufd2isanadaptorassistede3ligasetargetingunfoldedproteins
AT anitalehner ufd2isanadaptorassistede3ligasetargetingunfoldedproteins
AT linngazda ufd2isanadaptorassistede3ligasetargetingunfoldedproteins
AT karelstejskal ufd2isanadaptorassistede3ligasetargetingunfoldedproteins
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AT karlmechtler ufd2isanadaptorassistede3ligasetargetingunfoldedproteins
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AT timclausen ufd2isanadaptorassistede3ligasetargetingunfoldedproteins
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