Abstract
The covalent attachment of phosphate to either seryl or threonyl residues of proteins was identified first by F. Lipmann and P. A. Levene at the Rockefeller Institute for Medical Research (Rockefeller University, New York) in 1932; these researchers were interested in the chemical nature of acidic macromolecules present in the cell nucleus (paranucleic acid was the term used by Levene). This nuclear material was presumably a mixture of what we now call transcription factors. The enzyme responsible for this protein modification, casein kinase (phosvitin kinase), was subsequently found by M. Rabinowitz and Lipmann, but no obvious function was assigned for this enzyme. Another line of study focusing on glycogen metabolism initiated by C. F. Cori and G. T. Cori at St. Louis in the early 1940s, and by eminent investigators, such as E. W. Sutherland, T. W. Rall, E. G. Krebs, E. Fischer, and J. Larner, clarified the role of reversible phosphorylation in controlling the breakdown and resynthesis of glycogen.
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Nishizuka, Y., Kikkawa, U. (2003). Early Studies of Protein Kinase C. In: Newton, A.C. (eds) Protein Kinase C Protocols. Methods in Molecular Biology™, vol 233. Humana Press. https://doi.org/10.1385/1-59259-397-6:9
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DOI: https://doi.org/10.1385/1-59259-397-6:9
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