A non‐canonical scaffold‐type <scp>E3</scp> ligase complex mediates protein <scp>UFMylation</scp>-Reference-Cited by-同舟云学术

A non‐canonical scaffold‐type E3 ligase complex mediates protein UFMylation

Published:2022-09-19 Issue:21 Volume:41 Page:
ISSN:0261-4189
Container-title:The EMBO Journal
language:en
Short-container-title:The EMBO Journal

Author:

Peter Joshua J¹^ORCID,Magnussen Helge M¹^ORCID,DaRosa Paul A²,Millrine David¹,Matthews Stephen P¹,Lamoliatte Frederic¹,Sundaramoorthy Ramasubramanian³,Kopito Ron R²,Kulathu Yogesh¹^ORCID

Affiliation:

1. Medical Research Council Protein Phosphorylation & Ubiquitylation Unit (MRC‐PPU), School of Life Sciences University of Dundee Dundee UK

2. Department of Biology Stanford University Stanford CA USA

3. Centre for Gene Regulation and Expression, School of Life Sciences University of Dundee Dundee UK

Funder

National Institute of General Medical Sciences

Biotechnology and Biological Sciences Research Council

Publisher

EMBO

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Link

https://onlinelibrary.wiley.com/doi/pdf/10.15252/embj.2022111015

Reference84 articles.

1. Moyamoya disease factor RNF213 is a giant E3 ligase with a dynein-like core and a distinct ubiquitin-transfer mechanism

2. NEDD8 and ubiquitin ligation by cullin-RING E3 ligases

3. Decrypting UFMylation: How Proteins Are Modified with UFM1

4. Structural basis for the RING-catalyzed synthesis of K63-linked ubiquitin chains

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