CHIPping away at base excision repair.
In this issue of Molecular Cell, Parsons et al. (2008) report that the E3 ubiquitin ligase CHIP regulates the stability of the base excision repair (BER) proteins XRCC1 and DNA Pol beta, adding a new level of regulation for BER.
Sobol
Robert W
RW
Department of Pharmacology and Chemical Biology, University of Pittsburgh School of Medicine and University of Pittsburgh Cancer Institute, Hillman Cancer Center, Pittsburgh, PA 15213-1863, USA. rws9@pitt.edu
D000818:Animals; D004249:DNA Damage; D019951:DNA Polymerase beta / Q000235:genetics / Q000378:metabolism; D004260:DNA Repair; D004268:DNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D006801:Humans; D046911:Macromolecular Substances / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D044767:Ubiquitin-Protein Ligases / Q000235:genetics / Q000378:metabolism*; D000076105:X-ray Repair Cross Complementing Protein 1
D004268:DNA-Binding Proteins; D046911:Macromolecular Substances; D000076105:X-ray Repair Cross Complementing Protein 1; C000619371:XRCC1 protein, human; C467728:STUB1 protein, human; D044767:Ubiquitin-Protein Ligases; D019951:DNA Polymerase beta