Abstract
The discovery of the calcium-binding protein calmodulin in plants (Anderson and Cormier, 1978; Anderson et al., 1980) provided the basis for suggesting that Ca2+ serves a second messenger role in plants, and that Ca2+-dependent metabolic regulation in plant cells may be mediated by such Ca2+-binding proteins (Anderson et al., 1980). Support for these hypotheses has come from the demonstration that enzymes such as pea NAD kinase (Anderson and Cormier, 1978; Anderson et al., 1980) and Ca22+-transport ATPases of zucchini (Dieter and Marme, 1980) and corn (Dieter and Marme, 1981) are activated by calcium and calmodulin. Recently, several investigators have observed calcium-dependent and possibly calmodulin-dependent phosphorylation of endogenous proteins in plant extracts (Hetherington and Trewavas, 1982; Salimath and Marme, 1983; Veluthambi and Poovaiah, 1984a; 1984b; Putnam-Evans and Cormier, 1984). Also, Ca22+-dependent protein kinases have been partially purified from wheat germ (Polya and Davies, 1982 Polya et al., 1983; Polya and Micucci, 1984) and soybean cells (Putnam-Evans and Cormier, 1984). The regulation of protein phosphorylation by calcium may be a mechanism of metabolic and physiological control in plants, as it is in animals.
This work was supported by grants from the Department of Energy (DE-AS09-83ER13107) and the National Science Foundation (PCM-8213177).
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© 1986 Plenum Press, New York
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Putnam-Evans, C.L., Harmon, A.C., Cormier, M.J. (1986). Calcium-Dependent Protein Phosphorylation in Suspension-Cultured Soybean Cells. In: Trewavas, A.J. (eds) Molecular and Cellular Aspects of Calcium in Plant Development. NATO ASI Series, vol 104. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2177-4_13
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DOI: https://doi.org/10.1007/978-1-4613-2177-4_13
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