CCDC98 is a BRCA1-BRCT domain-binding protein involved in the DNA damage response
Abstract
The product of the breast cancer-1 gene, BRCA1, plays a crucial part in the DNA damage response through its interactions with many proteins, including BACH1, CtIP and RAP80. Here we identify a coiled-coil domain-containing protein, CCDC98, as a BRCA1-interacting protein. CCDC98 colocalizes with BRCA1 and is required for the formation of BRCA1 foci in response to ionizing radiation. Moreover, like BRCA1, CCDC98 has a role in radiation sensitivity and damage-induced G2/M checkpoint control. Together, these results suggest that CCDC98 is a mediator of BRCA1 function involved in the mammalian DNA damage response.
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Abraxas, Bach1, and CtIP directly interact with BRCA1 BRCT domains through the pSPxF motif in a phosphorylation-dependent manner, forming mutually exclusive A, B, and C complexes.
“Three proteins, Abraxas (also known as Abra1, FAM175A, CCDC98), Bach1 (also known as Brip1, FancJ) and CtIP (also known as RBBP8), directly interact with the BRCA1 BRCT domains through the pSPxF motif in a phosphorylation-dependent manner forming mutually exclusive complexes, which were thus named as the A, B and C complexes of BRCA1 (Greenberg et al., 2006; Kim et al., 2007; Liu et al., 2007;”
From The BRCA1-Interacting Protein Abraxas Is Required for Genomic Stability and Tumor Suppression (2014) · cites this paper as Kim et al., 2007
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Self-citation
- Authors
- Kim, H., Huang, J., & Chen, J.
- Affiliations
- Yale University (US)
- Corresponding author
- Chen, Junjie
- Venue
- Nature Structural & Molecular Biology
- Published
- 2007-07-22
- Volume
- 14
- Issue
- 8
- Pages
- 710-715
- ISSN
- 1545-9985 (ISSN-L)
- 1545-9993
- OpenAlex
- W2066606000
- Cited by
- 212
- References
- 24
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 3 · 2023: 22 · 2022: 7 · 2021: 8 · 2020: 6 · 2019: 7 · 2018: 8 · 2017: 8 · 2016: 12 · 2015: 8 · 2014: 16 · 2013: 15 · 2012: 19
- FWCI
- 6.50
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Structural & Molecular Biology (publishedVersion)
- PubMed (publishedVersion)
- Scholarworks@UNIST (Ulsan National Institute of Science and Technology) (submittedVersion)
- Funders
- National Cancer Institute (R01CA089239)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › BRCA gene mutations in cancer
- Health Sciences › Medicine › Oncology › PARP inhibition in cancer therapy
- Keywords
- BRCA1, DNA damage response, ionizing radiation, radiosensitivity, G2/M checkpoint, coiled-coil domain, protein-protein interaction
- MeSH terms
- Carrier Proteins, Cell Cycle, Cell Line, DNA Damage, DNA Repair, Humans, Signal Transduction, Protein Structure, Tertiary, BRCA1 Protein, Amino Acid Motifs, Protein Interaction Mapping
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