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Review

Nature Reviews Molecular Cell Biology 7, 323–334 (1 May 2006) | doi:10.1038/nrm1908

Regulation of DNA repair by ubiquitylation

Tony T. Huang & Alan D. D'Andrea

The process of ubiquitylation is best known for its role in targeting proteins for degradation by the proteasome. However, recent studies of DNA-repair and DNA-damage-response pathways have significantly broadened the scope of the role of ubiquitylation to include non-proteolytic functions of ubiquitin. These pathways involve the monoubiquitylation of key DNA-repair proteins that have regulatory functions in homologous recombination and translesion DNA synthesis, and involve the polyubiquitylation of nucleotide-excision-repair proteins.