Regulation of NF-κB signalling by the mono-ADP-ribosyltransferase ARTD10

Patricia Verheugd, Alexandra H. Forst, Larissa Milke, Nicolas Herzog, Karla L.H. Feijs, Elisabeth Kremmer, Henning Kleine and Bernhard Lüscher ()
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Patricia Verheugd: Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University
Alexandra H. Forst: Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University
Larissa Milke: Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University
Nicolas Herzog: Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University
Karla L.H. Feijs: Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University
Elisabeth Kremmer: Helmholtz Zentrum München, Institut für Molekulare Immunologie, Marchioninistrar. 25
Henning Kleine: Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University
Bernhard Lüscher: Institute of Biochemistry and Molecular Biology, Medical School, RWTH Aachen University

Nature Communications, 2013, vol. 4, issue 1, 1-11

Abstract: Abstract Adenosine diphosphate-ribosylation is a post-translational modification mediated by intracellular and membrane-associated extracellular enzymes and many bacterial toxins. The intracellular enzymes modify their substrates either by poly-ADP-ribosylation, exemplified by ARTD1/PARP1, or by mono-ADP-ribosylation. The latter has been discovered only recently, and little is known about its physiological relevance. The founding member of mono-ADP-ribosyltransferases is ARTD10/PARP10. It possesses two ubiquitin-interaction motifs, a unique feature among ARTD/PARP enzymes. Here, we find that the ARTD10 ubiquitin-interaction motifs bind to K63-linked poly-ubiquitin, a modification that is essential for NF-κB signalling. We therefore studied the role of ARTD10 in this pathway. ARTD10 inhibits the activation of NF-κB and downstream target genes in response to interleukin-1β and tumour necrosis factor-α, dependent on catalytic activity and poly-ubiquitin binding of ARTD10. Mechanistically ARTD10 interferes with poly-ubiquitination of NEMO, which interacts with and is a substrate of ARTD10. Our findings identify a novel regulator of NF-κB signalling and provide evidence for cross-talk between K63-linked poly-ubiquitination and mono-ADP-ribosylation.

Date: 2013
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DOI: 10.1038/ncomms2672

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