Allosteric control of Ubp6 and the proteasome via a bidirectional switch

• Published in: Nature communications Vol. 13; no. 1; pp. 838 - 13
• Main Authors: Hung, Ka Ying Sharon, Klumpe, Sven, Eisele, Markus R., Elsasser, Suzanne, Tian, Geng, Sun, Shuangwu, Moroco, Jamie A., Cheng, Tat Cheung, Joshi, Tapan, Seibel, Timo, Van Dalen, Duco, Feng, Xin-Hua, Lu, Ying, Ovaa, Huib, Engen, John R., Lee, Byung-Hoon, Rudack, Till, Sakata, Eri, Finley, Daniel
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 11.02.2022; Nature Publishing Group; Nature Portfolio
• Subjects: 101/28; 101/58; 631/45/474/2085; 631/45/474/2289; 631/535/1258/1259; 82/80; 82/83; Adenosine Triphosphatases - chemistry; Adenosine Triphosphatases - metabolism; Allosteric properties; Catalytic Domain; Conformation; Cryoelectron Microscopy; Cytoplasm; Endopeptidases - chemistry; Endopeptidases - genetics; Endopeptidases - metabolism; Grooves; Humanities and Social Sciences; multidisciplinary; Mutation; Proteasome Endopeptidase Complex - chemistry; Proteasome Endopeptidase Complex - genetics; Proteasome Endopeptidase Complex - metabolism; Proteasomes; Protein Conformation; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - genetics; Saccharomyces cerevisiae Proteins - metabolism; Science; Science (multidisciplinary); Substrates; Topology; Ubiquitin; Ubiquitin - metabolism; Ubiquitinated Proteins - metabolism; Yeast

The proteasome recognizes ubiquitinated proteins and can also edit ubiquitin marks, allowing substrates to be rejected based on ubiquitin chain topology. In yeast, editing is mediated by deubiquitinating enzyme Ubp6. The proteasome activates Ubp6, whereas Ubp6 inhibits the proteasome through deubiqu...