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Taming a protein destruction machine

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The evolutionarily conserved CUL4 E3 ubiquitin ligases, in concert with their DDB1 adaptor, regulate a diverse set of cellular processes including development, transcription, replication and DNA repair. Within the CRL4DDB2 ligase, DDB2 recruits the ligase to damaged DNA . CRL4 specificity is conferred upon by a set of more than a dozen substrate receptors, designated DCA Fs (DDB1 CUL4 Associated Factors). While DDB2 is specific for finding UV-induced DNA lesions in the genome, the remainder of the ligase receptors serve in pathways unrelated to DNA damage recognition. Using the CRL4DDB2 ligase as a model system, we studied targeting and regulation of this bi-functional nano-machine, investigating common architectural and functional traits amongst the modular CRL4 ligases. We recently also investigated how the Cop9 signalosome controls CRL function, and how small molecules such as the drug thalidomide impact ligase activity.

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