Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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3T3 Cells
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Animals
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Blotting, Western
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COP9 Signalosome Complex
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Cell Cycle Proteins / genetics
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Cell Cycle Proteins / metabolism*
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Cullin Proteins*
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Fungal Proteins / genetics
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Fungal Proteins / metabolism
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HeLa Cells
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Humans
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Mass Spectrometry
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Mice
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Multiprotein Complexes
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Mutation / genetics
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NEDD8 Protein
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Peptide Hydrolases
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Peptide Synthases / metabolism
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Protein Binding
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Protein Processing, Post-Translational
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Protein Subunits
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Proteins / chemistry
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Proteins / genetics
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Proteins / metabolism*
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Recombinant Fusion Proteins / metabolism
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SKP Cullin F-Box Protein Ligases
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Schizosaccharomyces / genetics
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Schizosaccharomyces / metabolism
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Substrate Specificity
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Swine
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Transfection
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Two-Hybrid System Techniques
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Ubiquitins / genetics
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Ubiquitins / metabolism*
Substances
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Cell Cycle Proteins
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Cullin 1
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Cullin Proteins
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Fungal Proteins
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Multiprotein Complexes
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NEDD8 Protein
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NEDD8 protein, human
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Nedd8 protein, mouse
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Protein Subunits
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Proteins
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Recombinant Fusion Proteins
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Ubiquitins
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SKP Cullin F-Box Protein Ligases
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Peptide Hydrolases
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COP9 Signalosome Complex
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Peptide Synthases