The ubiquitin-like modifier FAT10 interferes with SUMO activation

Annette Aichem (), Carolin Sailer, Stella Ryu, Nicola Catone, Nicolas Stankovic-Valentin, Gunter Schmidtke, Frauke Melchior, Florian Stengel and Marcus Groettrup
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Annette Aichem: Biotechnology Institute Thurgau at the University of Konstanz
Carolin Sailer: University of Konstanz
Stella Ryu: Biotechnology Institute Thurgau at the University of Konstanz
Nicola Catone: Biotechnology Institute Thurgau at the University of Konstanz
Nicolas Stankovic-Valentin: DKFZ-ZMBH Alliance
Gunter Schmidtke: University of Konstanz
Frauke Melchior: DKFZ-ZMBH Alliance
Florian Stengel: University of Konstanz
Marcus Groettrup: Biotechnology Institute Thurgau at the University of Konstanz

Nature Communications, 2019, vol. 10, issue 1, 1-17

Abstract: Abstract 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.

Date: 2019
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DOI: 10.1038/s41467-019-12430-z

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