DescriptionCtIP, a 125 kD protein, was originally found interacting with a transcription repressor, CtBP, through the PLDLS motif (CtBP-Interacting Protein) thus suggested a role in transcription. Studies have shown that CtIP also interacts with BRCA1 protein through the c-terminus BRCT domains also suggested that CtIP is a potential tumor suppressor. This CtIP-BRCA1 interaction can be disrupted by DNA damaging agents including UV or gamma-irradiation. Li et al (Nature 406, 210 - 215 (2000)) have shown that ATM phosphorylates CtIP at serine residues 664 and 745, and mutation of these sites abrogates the dissociation of BRCA1 from CtIP, resulting in persistent repression of BRCA1-dependent induction of GADD45 upon ionizing radiation.
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