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Casein kinase 2 binds to and phosphorylates BRCA1.
K A O'Brien1, S J Lemke, K S Cocke
1Lilly Research Laboratories, Eli Lilly and Company, Lilly Corporate Center, Indianapolis, Indiana, 46285-0424, USA.
Biochemical and Biophysical Research Communications
|July 15, 1999
Summary
Casein kinase 2 (CK2) interacts with the BRCA1 protein, a key player in DNA repair. This interaction, particularly phosphorylation at serine 1572, suggests CK2 regulates BRCA1 activity.
Area of Science:
- Biochemistry
- Molecular Biology
- Genetics
Background:
- The BRCA1 gene is crucial for DNA repair, transcription, and cell cycle regulation.
- BRCA1 protein phosphorylation is heightened after DNA damage or during cell cycle progression, suggesting a regulatory role.
Purpose of the Study:
- To investigate the interaction between BRCA1 and casein kinase 2 (CK2).
- To determine if CK2 can phosphorylate BRCA1 and identify the specific site involved.
Main Methods:
- Yeast two-hybrid assay to detect protein-protein interactions.
- Co-immunoprecipitation in Sf9 cells.
- In vitro kinase assays with purified proteins.
- Site-directed mutagenesis to identify phosphorylation sites.
Main Results:
- CK2 beta-subunit directly associates with the C-terminal region of BRCA1.
- This interaction is weakened by a missense mutation (M1775R) found in breast tumors.
- BRCA1 is phosphorylated in vitro by CK2, specifically at serine 1572.
Conclusions:
- CK2 binds to BRCA1 and phosphorylates it at serine 1572.
- CK2 is implicated as a potential regulator of BRCA1 activity.
- Understanding this interaction may offer insights into breast cancer development.