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Introduction: Protein kinase activation is pivotal in the signalling mechanism of many hormones, growth factors and neurotransmitters. Kinases are classified according to their substrate amino acids, i.e. serine/threonine specific or tyrosine specific. The regulators of serine/threonine-specific kinases include cyclic AMP (cAMP), cyclic GMP, Ca²⁺/calmodulin and Ca²⁺/phospholipid/diacylglycerol. Tyrosine-specific kinases are integral parts of the cytoplasmic domains of the receptors for many growth factors and are activated by binding of ligand.

An unavoidable conclusion from any study of cell signalling by kinases is that signals cannot be considered in isolation. Each signalling event ramifies into other signalling pathways. For example, the activity of adenylate cyclase which produces cAMP, and phosphodiesterases which hydrolyse cAMP, can be modulated independently by other signalling systems through their kinases (for review see Clemens et al. 1992). This commentary will review the effects of signalling through the Ca²⁺/phospholipid/diacylglycerol-dependent kinase (protein kinase

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