Publication details
Activation of the DNA-binding ability of latent p53 protein by protein kinase C is abolished by protein kinase CK2
| Authors | |
|---|---|
| Year of publication | 2004 |
| Type | Article in Periodical |
| Magazine / Source | Biochemical Journal |
| MU Faculty or unit | |
| Citation | |
| Field | Biochemistry |
| Keywords | Protein p53; Kinase; Phosphorylation; Piezoelectric biosensor |
| Description | Tumor suppressor protein p53 is one of the most important regulators of cell proliferation, differentiation and programmed cell death, triggering growth arrest and/or apoptosis in response to different cellular stress signals. The sequence-specific DNA binding function of p53 protein can be activated by several different stimuli modulating the C-terminal domain of this protein. The most likely physiological mechanism of p53 sequence-specific DNA binding activity is its post-translational modification, mainly phosphorylation of specific sites. Here we used non-radioactive electrophoretic mobility shift assay (EMSA) to show that C-terminal phosphorylation of p53 protein by cdk2/cyclin A at serine 315 and by PKC at serines 371, 376 and 378 can efficiently stimulate p53 binding to DNA in vitro as well as binding of C-terminal monoclonal antibody Bp53-10 recognizing the residue 371-380. |
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