DET1-mediated degradation of a SAGA-like deubiquitination module controls H2Bub homeostasis

作者：Amr Nassrallah, Martin Rougée, Clara Bourbousse, Stéphanie Drevensek, Sandra Fonseca, Elisa Iniesto, Ouardia Aït-Mohamed, Anne-Flore Deton-Cabanillas, Gérald Zabulon, Ikhlak Ahmed, David Stroebel, Vanessa Masson, Bérangère Lombard, Dominique Eeckhout, Kris Gevaert, Damarys Loew, Auguste Genovesio, Cécile Breyton, Geert De Jaeger, Chris Bowler, Vicente Rubio, Fredy Barnèche · 发表于：eLife · 年份：2018 · DOI：10.7554/elife.37892 · 被引用次数：132 · 研究领域：Ubiquitin and proteasome pathways、Plant Molecular Biology Research、Cancer, Hypoxia, and Metabolism

DE-ETIOLATED 1 (DET1) is an evolutionarily conserved component of the ubiquitination machinery that mediates the destabilization of key regulators of cell differentiation and proliferation in multicellular organisms. In this study, we provide evidence from Arabidopsis that DET1 is essential for the regulation of histone H2B monoubiquitination (H2Bub) over most genes by controlling the stability of a deubiquitination module (DUBm). In contrast with yeast and metazoan DUB modules that are associated with the large SAGA complex, the Arabidopsis DUBm only comprises three proteins (hereafter named SGF11, ENY2 and UBP22) and appears to act independently as a major H2Bub deubiquitinase activity. Our study further unveils that DET1-DDB1-Associated-1 (DDA1) protein interacts with SGF11 in vivo, linking the DET1 complex to light-dependent ubiquitin-mediated proteolytic degradation of the DUBm. Collectively, these findings uncover a signaling path controlling DUBm availability, potentially adjusting H2Bub turnover capacity to the cell transcriptional status.