Promotion of NEDD8-CUL1 Conjugate Cleavage by COP9 Signalosome

• Published in: Science (American Association for the Advancement of Science) Vol. 292; no. 5520; pp. 1382 - 1385
• Main Authors: Lyapina, Svetlana, Cope, Gregory, Shevchenko, Anna, Serino, Giovanna, Tsuge, Tomohiko, Zhou, Chunshui, Wolf, Dieter A., Wei, Ning, Shevchenko, Andrej, Deshaies, Raymond J.
• Format: Journal Article
• Language: English
• Published: Washington, DC American Society for the Advancement of Science 18.05.2001; American Association for the Advancement of Science; The American Association for the Advancement of Science
• Subjects: 3T3 cells; Antibodies; Art and archaeology; COP9 signalosome; CUL1 protein; Flowers & plants; HeLa cells; Lipids; NEDD8 protein; Phospholipids; Plant cells; Plasmids; Proteins; Schizosaccharomyces pombe; Scientific Concepts; Ubiquitin; Ubiquitins; Western blotting; Yeasts; United States
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.1059780

SCF ubiquitin ligases control various processes by marking regulatory proteins for ubiquitin-dependent proteolysis. To illuminate how SCF complexes are regulated, we sought proteins that interact with the human SCF component CUL1. The COP9 signalosome (CSN), a suppressor of plant photomorphogenesis, associated with multiple cullins and promoted cleavage of the ubiquitin-like protein NEDD8 from Schizosaccharomyces pombe CUL1 in vivo and in vitro. Multiple NEDD8-modified proteins uniquely accumulated in CSN-deficient S. pombe cells. We propose that the broad spectrum of activities previously attributed to CSN subunits-including repression of photomorphogenesis, activation of JUN, and activation of p27 nuclear export-underscores the importance of dynamic cycles of NEDD8 attachment and removal in biological regulation.