| Summary: | Protein kinase CK2 (also known as Casein Kinase II) is a protein serine/threonine kinase. It is an ubiquitously distributed tetrameric enzyme composed of two catalytic subunits ($\alpha$ and/or $\alpha\sp\prime$) and two regulatory subunits ($\beta$). The $\alpha$ and $\alpha\sp\prime$ are quite similar except their carboxyl termini. The precise role of CK2 in biological responses remains to be characterized, but a great deal of recent evidence indicates that CK2 is involved in the regulation of proliferative events. As a first step towards determining whether the phosphorylation of CK2 is important for cell division, Cos-7 cells have been transfected with cDNAs encoding wild type or non-phosphorylatable mutants of CK2$\alpha,$ CK2$\alpha\sp\prime$ or CK2$\beta .$ To discriminate between the transfected CK2$\alpha,$ CK2$\alpha\sp\prime$ or CK2$\beta$ and their endogenous counterparts, the cDNAs have been modified by the addition of different epitope tags at the amino or carboxyl terminus. The studies described in this thesis are an important prelude to a systematic examination of the functional role of CK2 and its phosphorylation during cell cycle progression. (Abstract shortened by UMI.)
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