The ubiquitin-like modifier FAT10 – much more than a proteasome-targeting signal
Author:
Affiliation:
1. Biotechnology Institute Thurgau at the University of Konstanz, CH-8280 Kreuzlingen, Switzerland
2. Division of Immunology, Department of Biology, University of Konstanz, D-78457 Konstanz, Germany
Abstract
Funder
Deutsche Forschungsgemeinschaft
Velux Stiftung
Swiss State Secretariat for Education, Research and Innovation
Publisher
The Company of Biologists
Subject
Cell Biology
Link
http://journals.biologists.com/jcs/article-pdf/doi/10.1242/jcs.246041/2024635/jcs246041.pdf
Reference147 articles.
1. USE1 is a bispecific conjugating enzyme for ubiquitin and FAT10, which FAT10ylates itself in cis;Aichem;Nat. Commun.,2010
2. The proteomic analysis of endogenous FAT10 substrates identifies p62/SQSTM1 as a substrate of FAT10ylation;Aichem;J. Cell Sci.,2012
3. Investigations into the auto-FAT10ylation of the bispecific E2 conjugating enzyme UBA6-specific E2 enzyme 1;Aichem;FEBS J.,2014
4. The structure of the ubiquitin-like modifier FAT10 reveals an alternative targeting mechanism for proteasomal degradation;Aichem;Nat. Commun.,2018
5. The ubiquitin-like modifier FAT10 interferes with SUMO activation;Aichem;Nat. Commun.,2019
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