The mechanism of signal transduction at the insulin receptor has long been one of the major questions of cellular endocrinology. No general relationship has been established with any of the well-known second messenger systems such as cyclic AMP, calcium or phosphoinositides (reviewed by Goldfine, 1987); a fundamentally different signalling pathway is therefore presumably involved. The same is apparently true of the stimulation of cell growth by the insulin-like growth factors (IGFs), which frequently exhibit synergy with agonists which activate the established second messenger pathways (Rozengurt, 1986).
The insulin and type-I IGF receptors are structurally-similar βααβ heterotetramers, and possess protein-tyrosine kinases in their intracellular domains (Kasuga, Karlsson & Kahn, 1982; Jacobs, Kull, Earp et al. 1983). This suggests that a cascade of regulatory phosphorylation events, initiated by the catalytic domain, might answer the question of mechanism. Many proteins do indeed undergo changes in phosphorylation in response to insulin or IGF (reviewed
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