Mechanisms of Receptor-coupled Signal Transduction

  • Richard A. Cerione
Part of the Wenner-Gren Center International Symposium Series book series (WGCISS)


The mechanisms by which specific cell surface receptor proteins transmit signals to enzymes, transport proteins or other biological effectors has been the subject of extensive investigation. Among the most studied of these receptor-coupled signal transduction systems have been those involved in the adrenergic regulation of adenylate cyclase activity. Most of the primary components of the catecholamine-mediated stimulatory and inhibitory pathways of adenylate cyclase have now been purified. Both stimulation and inhibition of the enzyme activity is initiated by the binding of hormones to specific receptors; the β-adrenergic receptor being involved in stimulation while the α2-adrenergic receptor is responsible for triggering inhibition of the enzyme activity. Each of these receptors is known to be comprised of a single type of polypeptide with an apparent Mr ≅ 65,000 daltons (Benovic et al., 1984; Regan et al., 1986). Following their interaction with hormones, these receptors go on to interact with, and promote the activation of, distinct GTP binding proteins which are typically designated as Ns or Gs (the stimulatory GTP binding protein) and Ni or Gi (the innibitory GTP binding protein). Both Ns and Ni are heterotrimeric in structure.


Insulin Receptor Adenylate Cyclase Adenylate Cyclase Activity GTPase Activity Phospholipid Vesicle 
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© The Wenner-Gren Center 1987

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  • Richard A. Cerione

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