The conserved protein DCN-1/Dcn1p is required for cullin neddylation in C. elegans and S. cerevisiae

Thimo Kurz, Nurhan Özlü, Fabian Rudolf, Sean M. O'Rourke, Brian Luke, Kay Hofmann, Anthony A. Hyman, Bruce Bowerman () and Matthias Peter ()
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Thimo Kurz: Institute of Biochemistry, ETH Hönggerberg
Nurhan Özlü: Max Planck Institute of Molecular Cell Biology and Genetics
Fabian Rudolf: Institute of Biochemistry, ETH Hönggerberg
Sean M. O'Rourke: University of Oregon
Brian Luke: Institute of Biochemistry, ETH Hönggerberg
Kay Hofmann: Memorec Biotec GmbH
Anthony A. Hyman: Max Planck Institute of Molecular Cell Biology and Genetics
Bruce Bowerman: University of Oregon
Matthias Peter: Institute of Biochemistry, ETH Hönggerberg

Nature, 2005, vol. 435, issue 7046, 1257-1261

Abstract: Abstract SCF-type E3 ubiquitin ligases are multi-protein complexes required for polyubiquitination and subsequent degradation of target proteins by the 26S proteasome1. Cullins, together with the RING-finger protein Rbx1, form the catalytic core of the ligase, and recruit the substrate-recognition module1,2,3,4. Cycles of covalent modification of cullins by the ubiquitin-like molecule Nedd8 (neddylation)5 and removal of Nedd8 by the COP9 signalosome (deneddylation) positively regulate E3 ligase activity6,7. Here we report the identification and analysis of a widely conserved protein that is required for cullin neddylation in the nematode Caenorhabditis elegans and the yeast Saccharomyces cerevisiae. C. elegans DCN-1 and S. cerevisiae Dcn1p (defective in cullin neddylation) are characterized by a novel UBA-like ubiquitin-binding domain and a DUF298 domain of unknown function. Consistent with their requirements for neddylation, DCN-1 and Dcn1p directly bind Nedd8 and physically associate with cullins in both species. Moreover, overexpression of Dcn1p in yeast results in the accumulation of Nedd8-modified cullin Cdc53p. Both in vivo and in vitro experiments indicate that Dcn1p does not inhibit deneddylation of Cdc53p by the COP9 signalosome, but greatly increases the kinetics of the neddylation reaction.

Date: 2005
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DOI: 10.1038/nature03662

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