
pmid: 21550341
The DDB1–DDB2–CUL4–RBX1 complex serves as the primary detection device for UV‐induced lesions in the genome. It simultaneously functions as a CUL4 type E3 ubiquitin ligase. We review the current understanding of this dual function ubiquitin ligase and damage detection complex. The DDB2 damage binding module is merely one of a large family of possible DDB1–CUL4 associated factors (DCAF), most of which are substrate receptors for other DDB1–CUL4 complexes. DDB2 and the Cockayne‐syndrome A protein (CSA) function in nucleotide excision repair, whereas the remaining receptors operate in a wide range of other biological pathways. We will examine the modular architecture of DDB1–CUL4 in complex with DDB2, CSA and CDT2 focusing on shared architectural, targeting and regulatory principles.
DNA Repair, Models, Genetic, Genome, Human, Ultraviolet Rays, Ubiquitin-Protein Ligases, DDB2, Nuclear Proteins, CSA, Cullin Proteins, DNA-Binding Proteins, CUL4, DNA Repair Enzymes, Genome stability, Humans, CDT2, DNA Damage, Transcription Factors
DNA Repair, Models, Genetic, Genome, Human, Ultraviolet Rays, Ubiquitin-Protein Ligases, DDB2, Nuclear Proteins, CSA, Cullin Proteins, DNA-Binding Proteins, CUL4, DNA Repair Enzymes, Genome stability, Humans, CDT2, DNA Damage, Transcription Factors
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