RAP80 responds to DNA damage induced by both ionizing radiation and UV irradiation and is phosphorylated at Ser 205.

ABSTRACT: Receptor-associated protein (RAP80), a nuclear protein containing two ubiquitin-interacting motifs (UIM), was recently found to be associated with breast cancer-1 (BRCA1) and to translocate to ionizing radiation-induced foci (IRIF). In this study, we show that the BRCT mutant of BRCA1, R1699W, which is associated with increased risk of breast cancer, is unable to interact with RAP80. Previously, we showed that ataxia-telangiectasia mutated protein kinase (ATM) can phosphorylate RAP80 in vitro at Ser(205), but whether this site is a target of ATM in whole cells was not established. To address this question, we generated an anti-RAP80Ser205(P) antibody that specifically recognizes RAP80 phosphorylated at Ser(205). Our data show that RAP80 becomes phosphorylated at Ser(205) in cells exposed t

SUBMITTER: Yan J 

PROVIDER: S-EPMC2769268 | biostudies-literature | 2008 Jun

REPOSITORIES: biostudies-literature