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Phosphorylation of casein kinase II by p34cdc2 in vitro and at mitosis.

Litchfield, D W and Lüscher, B and Lozeman, F J and Eisenman, R N and Krebs, E G (1992) Phosphorylation of casein kinase II by p34cdc2 in vitro and at mitosis. The Journal of biological chemistry, 267 (20). pp. 13943-13951. ISSN 0021-9258

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Article URL: http://www.jbc.org/cgi/reprint/267/20/13943

Abstract

In human epidermal carcinoma A431 cells, the beta subunit of casein kinase II is phosphorylated at an autophosphorylation site and at serine 209 which can be phosphorylated in vitro by p34cdc2 (Litchfield, D. W., Lozeman, F. J., Cicirelli, M. F., Harrylock, M., Ericsson, L. H., Piening, C. J., and Krebs, E. G. (1991) J. Biol. Chem. 266, 20380-20389). Given the importance of p34cdc2 in the regulation of cell cycle events, we were interested in examining the phosphorylation of casein kinase II during different stages of the cell cycle. In this study it is demonstrated that the extent of phosphorylation of serine 209 in the beta subunit is significantly increased relative to phosphorylation of the autophosphorylation site when chicken bursal lymphoma BK3A cells are arrested at mitosis by nocodazole treatment. This result suggests that serine 209 is a likely physiological target for p34cdc2. In addition, the alpha subunit of casein kinase II also undergoes dramatic phosphorylation with an associated alteration in its electrophoretic mobility when BK3A cells or human Jurkat cells are arrested with nocodazole. Phosphopeptide mapping studies indicate that p34cdc2 can phosphorylate in vitro the same peptides on the alpha subunit that are phosphorylated in cells arrested at mitosis. These phosphorylation sites were localized to serine and threonine residues in the carboxyl-terminal domain of alpha. Taken together, the results of this study indicate that casein kinase II is a probable physiological substrate for p34cdc2 and suggest that its functional properties could be affected in a cell cycle-dependent manner.

Item Type: Article
Additional Information: This article is freely available at the journal's website.
PubMed ID: 1629192
Grant Numbers: DK45258, GM42508, CA20525, Terry Fox Team Development Grant
Keywords or MeSH Headings: Animals; Antibodies; CDC2 Protein Kinase/metabolism; Carcinoma, Squamous Cell; Casein Kinase II; Cattle; Cell Line; Chickens; Chromatography, Ion Exchange; Humans; Lymphoma; Macromolecular Substances; Male; Mitosis/physiology; Peptide Mapping; Phosphopeptides/isolation & purification; Phosphorylation; Protein-Serine-Threonine Kinases/isolation & purification/metabolism; Testis/enzymology; Trypsin;
Subjects: Molecules > Proteins > Enzymes
Cellular and Organismal Processes > Cell Physiology > Cell cycle
Molecules > Proteins > Cell cycle proteins
Depositing User: Library Staff
Date Deposited: 02 Dec 2008 21:59
Last Modified: 21 May 2010 22:57
URI: http://authors.fhcrc.org/id/eprint/139

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