The ubiquitin-like modifier FAT10 interferes with SUMO activation
The covalent attachment of the cytokine-inducible ubiquitin-like modifier HLA-F adjacent transcript 10 (FAT10) to hundreds of substrate proteins leads to their rapid degradation by the 26 S proteasome independently of ubiquitylation. Here, we identify another function of FAT10, showing that it inter...
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| Hauptverfasser: | , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
01 October 2019
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| In: |
Nature Communications
Year: 2019, Jahrgang: 10 |
| ISSN: | 2041-1723 |
| DOI: | 10.1038/s41467-019-12430-z |
| Online-Zugang: | Verlag, Volltext: https://doi.org/10.1038/s41467-019-12430-z Verlag: https://www.nature.com/articles/s41467-019-12430-z 
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| Verfasserangaben: | Annette Aichem, Carolin Sailer, Stella Ryu, Nicola Catone, Nicolas Stankovic-Valentin, Gunter Schmidtke, Frauke Melchior, Florian Stengel & Marcus Groettrup |
MARC
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| 520 | |a The covalent attachment of the cytokine-inducible ubiquitin-like modifier HLA-F adjacent transcript 10 (FAT10) to hundreds of substrate proteins leads to their rapid degradation by the 26 S proteasome independently of ubiquitylation. Here, we identify another function of FAT10, showing that it interferes with the activation of SUMO1/2/3 in vitro and down-regulates SUMO conjugation and the SUMO-dependent formation of promyelocytic leukemia protein (PML) bodies in cells. Mechanistically, we show that FAT10 directly binds to and impedes the activity of the heterodimeric SUMO E1 activating enzyme AOS1/UBA2 by competing very efficiently with SUMO for activation and thioester formation. Nevertheless, activation of FAT10 by AOS1/UBA2 does not lead to covalent conjugation of FAT10 with substrate proteins which relies on its cognate E1 enzyme UBA6. Hence, we report that one ubiquitin-like modifier (FAT10) inhibits the conjugation and function of another ubiquitin-like modifier (SUMO) by impairing its activation. | ||
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