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NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases.

Molecular cell | Dec 30, 2002

http://www.ncbi.nlm.nih.gov/pubmed/12504025

Cullin proteins assemble a large number of RING E3 ubiquitin ligases and regulate various physiological processes. Covalent modification of cullins by the ubiquitin-like protein NEDD8 activates cullin ligases through an as yet undefined mechanism. We show here that p120(CAND1) selectively binds to unneddylated CUL1 and is dissociated by CUL1 neddylation. CAND1 formed a ternary complex with CUL1 and ROC1. CAND1 dissociated SKP1 from CUL1 and inhibited SCF ligase activity in vitro. Suppression of CAND1 in vivo increased the level of the CUL1-SKP1 complex. We suggest that by restricting SKP1-CUL1 interaction, CAND1 regulated the assembly of productive SCF ubiquitin ligases, allowing a common CUL1-ROC core to be utilized by a large number of SKP1-F box-substrate subcomplexes.

Pubmed ID: 12504025 RIS Download

Mesh terms: Amino Acid Sequence | Bacterial Proteins | Carrier Proteins | Cell Cycle Proteins | Cullin Proteins | DNA-Binding Proteins | Enzyme Inhibitors | F-Box Proteins | Genes, myc | Humans | Kinetics | Ligases | Macromolecular Substances | Molecular Sequence Data | Mutagenesis, Site-Directed | Peptide Synthases | Recombinant Proteins | SKP Cullin F-Box Protein Ligases | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Transcription Factors | Ubiquitins

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Addgene (Reagent, Plasmid)

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