Regular ArticleCasein Kinase 2 Binds to and Phosphorylates BRCA1☆
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Cited by (44)
Predicting CK2 beta-dependent substrates using linear patterns
2015, Biochemistry and Biophysics ReportsCitation Excerpt :In addition, protein overlap points to a possible link between cytoplasmic class-III substrates phosphorylation and their redistribution to the nucleus. The involvement of CK2 in DNA repair and its regulation has been well-documented with the identification for instance of BRCA1, APC and P53 as binding partners and/or substrates of the enzyme [64–66]. The biological process enrichment analysis (S5 File) supports a possible functional relationship between beta-dependent phosphorylation and the response to DNA damage stimulus and DNA repair.
The BRCA1 ubiquitin ligase and homologous recombination repair
2011, FEBS LettersCitation Excerpt :Importantly SUMO modification of BRCA1 significantly increases the E3 ligase activity of BRCA1–BARD1 heterodimer in vitro, and mutations at the sumoylation sites of BRCA1, K199R and E121R, dramatically reduced the conjugated ubiquitin foci formation [107]. BRCA1 is phosphorylated by several kinases involved in either cell cycle regulation or DNA damage response, including CDK2, ATM, ATR, Chk2, and CK2 [108–112]. BARD1 is also phosphorylated by CDK2, or at ATM/ATR consensus sites in response to DNA damage [113,114].
Protein kinase CK2 catalyzes tyrosine phosphorylation in mammalian cells
2008, Cellular SignallingInduction of cell death in antiestrogen resistant human breast cancer cells by the protein kinase CK2 inhibitor DMAT
2007, Cancer LettersCitation Excerpt :The regulation of Wnt signaling by CK2 is probably not the only contribution of CK2 to mammary tumorigenesis and survival. CK2 phosphorylates and regulates many other substrates, including the estrogen receptor α (ERα) [20], the transcription factor NF-κB [21], breast cancer susceptibility gene 1 (BRCA1) [22], the tumor suppressor protein p53 [23], the p53 regulator HDM2 [24] and PTEN [25] all with the potential of influencing breast cancer development. Moreover, CK2 interacts with and phosphorylates the protein kinase Akt at a site different from the major activation sites (Thr308 and Ser374), but still resulting in enhanced Akt activity [26,27].
The role of protein kinases in pancreatic carcinogenesis
2007, Clinica Chimica ActaPhosphorylation of ICBP90 by protein kinase A enhances topoisomerase IIα expression
2004, Biochemical and Biophysical Research Communications
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Abbreviations used: aa, amino acid; R or Arg, arginine; β-gal, β-galactosidase; BRCA1, breast cancer susceptibility gene; C-terminus, carboxy terminus; CK2, casein kinase 2; DBD, DNA binding domain; GST, glutathione S-transferase; Hepes, N-2-hydroxyethylpiperazine-N-2-ethanesulfonic acid, M or Met, methionine; moi, multiplicity of infection; S or Ser, serine; SDS–PAGE, sodium dodecyl sulfate–polyacrylamide gel electrophoresis; Y2H, yeast two hybrid
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Present address: Endocrine Research Division, Lilly Research Laboratories, Indianapolis, IN 46285-0434.
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Present address: Clinical Laboratory Medicine, Lilly Research Laboratories, Indianapolis, IN 46285-1543.
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To whom correspondence should be addressed. Fax: (317) 276-9086. E-mail: [email protected].