Cdk1 Protein-mediated Phosphorylation of Receptor-associated Protein 80 (RAP80) Serine 677 Modulates DNA Damage-induced G(2)/M Checkpoint and Cell Survivalopen access
- Authors
- Cho, Hyun Jung; Oh, Yun Jung; Han, Seung Hun; Chung, Hee Jin; Kim, Chang Hee; Lee, Nam Soo; Kim, Won-Ju; Choi, Je-Min; Kim, Hongtae
- Issue Date
- Feb-2013
- Publisher
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
- Citation
- JOURNAL OF BIOLOGICAL CHEMISTRY, v.288, no.6, pp.3768 - 3776
- Indexed
- SCIE
SCOPUS
- Journal Title
- JOURNAL OF BIOLOGICAL CHEMISTRY
- Volume
- 288
- Number
- 6
- Start Page
- 3768
- End Page
- 3776
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/163520
- DOI
- 10.1074/jbc.M112.401299
- ISSN
- 0021-9258
- Abstract
- Post-translational phosphorylation plays critical roles in the assembly of signaling and repair proteins in the DNA damage response pathway. RAP80, a component of the BRCA1-A complex, is crucial in cell cycle checkpoint activation and DNA damage repair. However, its molecular mechanism is unclear. In this study, we identified Cdk1 as a new RAP80-binding protein and demonstrated that the Cdk1-cyclin B-1 complex phosphorylates RAP80 at Ser-677 using an in vitro kinase assay and a phosphopeptide-specific antibody against phospho-Ser-677 of RAP80. RAP80 Ser-677 phosphorylation occurred in the M phase of the cell cycle when Cdk1 was in an active state. In addition, ionizing radiation (IR) induced RAP80 phosphorylation at Ser-677. Mutation of Ser-677 to alanine sensitized cells to IR and functioned in G(2)/M checkpoint control. These results suggest that post-translational phosphorylation of RAP80 by the Cdk1-cyclin B-1 complex is important for RAP80 functional sensitivity to IR and G(2)/M checkpoint control.
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