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Evolutionary Tinkering in Gene Expression pp 59–69Cite as

Ca2+-Calmodulin-Dependent Protein Kinases and Protein Kinase C: Functional Similarities

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Part of the book series: NATO ASI Series ((volume 169))

Abstract

Protein serine and threonine kinases can be classified into individual groups or subclasses on the basis of the type of regulation of their activities (Krebs, 1986). Two of the most intensively studied groups are Ca2+-regulated, i.e. the Ca2+/calmodulin (CaM)-dependent and the Ca2+-phospholipid (diacylglycerol)-dependent protein kinases. Of the enzymes belonging in the category of Ca2+/CaM-dependent kinases, myosin light chain kinases (MLCK) are distinguished by their high degree of substrate specificity and CaM dependency (Edelman et al, 1987). Phosphorylase kinase (PhK) another member of the same group is characterized by a broader substrate specificity. Its primary substrate is phosphorylase b but the enzyme may catalyze the phosphorylation of other proteins (Chan & Graves, 1984). In addition, a number of Ca2+/CaM-dependent multifunctional protein kinases (Ca2+/CaM PrK) identified in a variety of tissues shows a broad substrate specificity suggesting that such a group of CaM-dependent protein kinases may play important roles in the control of different cellular processes (Shenolikar et al, 1986). On the other hand, protein kinase C (PKC) is a multifunctional protein kinase identified by Nishizuka and co-workers as a Ca2+- and phospholipid-dependent protein kinase that plays a crucial role in the signal transduction for a variety of biologically active substances involved in cellular function and proliferation (Nishizuka, 1984). In the presence of limiting amounts of Ca2+ and phospholipids its activity is stimulated by sn-1,2-diacylglecerols or by phorbol esters (Nishizuka, 1984) and the kinase phosphorylates a broad range of cellular proteins (Kikkawa and Nishizuka, 1986).

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Authors and Affiliations

  1. The National Hellenic Research Foundation, 48 Vassileos Constantinou Avenue, Athens, 116 35, Greece

    Theodore G. Sotiroudis, Symeon M. Kyriakidis, Leonidas G. Baltas, Vasilis G. Zevgolis & Athanasios E. Evangelopoulos

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  1. Theodore G. Sotiroudis
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  2. Symeon M. Kyriakidis
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  3. Leonidas G. Baltas
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  4. Vasilis G. Zevgolis
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  5. Athanasios E. Evangelopoulos
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Editors and Affiliations

  1. Institut de Biologie Physico-Chimique, Paris, France

    Marianne Grunberg-Manago

  2. Aarhus University, Aarhus, Denmark

    Brian F. C. Clark

  3. University of Munich, Munich, Federal Republic of Germany

    Hans G. Zachau

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© 1989 Plenum Press, New York

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Sotiroudis, T.G., Kyriakidis, S.M., Baltas, L.G., Zevgolis, V.G., Evangelopoulos, A.E. (1989). Ca2+-Calmodulin-Dependent Protein Kinases and Protein Kinase C: Functional Similarities. In: Grunberg-Manago, M., Clark, B.F.C., Zachau, H.G. (eds) Evolutionary Tinkering in Gene Expression. NATO ASI Series, vol 169. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-5664-6_6

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  • DOI: https://doi.org/10.1007/978-1-4684-5664-6_6

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