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Gliotoxin Suppresses NF-κB Activation by Selectively Inhibiting Linear Ubiquitin Chain Assembly Complex (LUBAC)

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Graduate School of Pharmaceutical Sciences, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan
Open Innovation Center for Drug Discovery, The University of Tokyo, 7-3-1 Hongo, Bunkyo-ku, Tokyo 113-0033, Japan
§ Department of Molecular Cell Biology, Graduate School of Medicine, Osaka City University, Osaka 545-8585, Japan
Structural Biology Research Center, Photon Factory, Institute of Materials Structure Science, High-Energy Accelerator Research Organization (KEK), Tsukuba, Ibaraki 305-8501, Japan
Medical Innovation Center Laboratory for Malignancy Control Research/DSK, Graduate School of Medicine, Kyoto University, Yoshida-Konoe-cho, Sakyo-ku, Kyoto-shi, Kyoto 606-8501, Japan
# Department of Structural Biology, Stanford University School of Medicine, Stanford, California 94305, United States
SLAC National Accelerator Laboratory, Menlo Park, California 94025, United States
Department of Biophysics and Biochemistry, Graduate School of Medicine, Osaka University, Suita, Osaka 565-0871, Japan
Graduate School of Medicine, Kyoto University, Yoshida-Konoe-cho, Sakyo-ku, Kyoto-shi, Kyoto 606-8501, Japan
Cite this: ACS Chem. Biol. 2015, 10, 3, 675–681
Publication Date (Web):December 10, 2014
Copyright © 2014 American Chemical Society

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    A linear ubiquitin chain, which consists of ubiquitin molecules linked via their N- and C-termini, is formed by a linear ubiquitin chain assembly complex (LUBAC) composed of HOIP, HOIL-1L, and SHARPIN, and conjugation of a linear ubiquitin chain on the NF-κB essential modulator (NEMO) is deeply involved in NF-κB activation induced by various signals. Since abnormal activation of NF-κB is associated with inflammatory disease and malignancy, we searched for an inhibitor of LUBAC by high-throughput screening (HTS) with a Tb3+-fluorescein FRET system. As a result, we found that the fungal metabolite gliotoxin inhibits LUBAC selectively by binding to the RING-IBR-RING domain of HOIP, the catalytic center of LUBAC. Gliotoxin has been well-known as an inhibitor of NF-κB activation, though its action mechanism has remained elusive. Here, we show that gliotoxin inhibits signal-induced NF-κB activation by selectively inhibiting LUBAC-mediated linear ubiquitin chain formation.

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