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The ubiquitin-like modifier FAT10 interferes with SUMO activation

ABSTRACT: In this study, the proteins SumoE1 and Fat10 or Fat10-AV mutant were crosslinked using the crosslinking reagent H12/D12 BS3 in order to determine specific interaction sites of Fat10 and SumoE1. Furthermore, quantitative chemical crosslinking coupled to mass spectrometry (q-XL-MS) was used to compare crosslink abundances of SumoE1 in presence of Sumo as well as Sumo and Fat10 versus crosslink abundances of SumoE1 in absence of Sumo and Fat10 in order to determine the influence of Sumo and Fat10 on the structural dynamics of SumoE1.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: Florian Stengel

LAB HEAD: Florian Stengel

PROVIDER: PXD012592 | Pride | 2019-10-08

REPOSITORIES: Pride

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			Action	DRS
	F1801_sailerc_031.raw	Raw
	F1801_sailerc_032.raw	Raw
	F1801_sailerc_033.raw	Raw
	F1801_sailerc_034.raw	Raw
	F1903_sailerc_185.raw	Raw

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The ubiquitin-like modifier FAT10 interferes with SUMO activation.

Aichem Annette A Sailer Carolin C Ryu Stella S Catone Nicola N Stankovic-Valentin Nicolas N Schmidtke Gunter G Melchior Frauke F Stengel Florian F Groettrup Marcus M

Nature communications 20191001 1

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 t ...[more]

PMID: 31575873

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