Binding Domain for p21WAF1 on the Polypeptide Chain of the Protein Kinase CK2 β-Subunit

Protein kinase CK2 is a ubiquitous serine/threonine kinase which is involved in many proliferation-related processes in the cell. It is composed of two regulatory β-subunits and two catalytic α-subunits. Its regulation still remains mysterious in spite of many years of intense research. One of its r...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2000-02, Vol.268 (3), p.882-885
Main Authors: Götz, Claudia, Kartarius, Sabine, Scholtes, Petra, Montenarh, Mathias
Format: Article
Language:English
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Summary:Protein kinase CK2 is a ubiquitous serine/threonine kinase which is involved in many proliferation-related processes in the cell. It is composed of two regulatory β-subunits and two catalytic α-subunits. Its regulation still remains mysterious in spite of many years of intense research. One of its regulators is the cdk inhibitory molecule p21WAF1—a protein which is expressed in situations of genotoxic stress. p21WAF1 binds to the β-subunit of CK2 and inhibits the activity of CK2. Using deletion mutants of CK2 β as well as a peptide library consisting of 15-amino-acid-long peptides derived from the polypeptide chain of CK2 β we mapped the binding region for p21WAF1 on the polypeptide chain of CK2 β. We localized an amino-terminal and a carboxy-terminal binding domain. Binding of p21WAF1 to both regions of the CK2 β-subunit interferes with the phosphotransferase activity of the CK2 holoenzyme.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.2000.2230