The role of hormone receptors and GTP-regulatory proteins in membrane transduction

@article{Rodbell1980TheRO,
  title={The role of hormone receptors and GTP-regulatory proteins in membrane transduction},
  author={Martin Rodbell},
  journal={Nature},
  year={1980},
  volume={284},
  pages={17-22}
}
Cell membrane receptors for hormones and neurotransmitters form oligomeric complexes with GTP-regulatory proteins and inhibit the latter from reacting with GTP. Hormones and neurotransmitters act by releasing the inhibitory constraints imposed by the receptors, thus allowing the GTP-regulatory proteins to interact with and control the activity of enzymes such as adenylate cyclase. This theory may apply generally to membrane signal transduction involving surface receptors. 

Regulation of the Responsiveness of Adenylate Cyclase to Catecholamines

Cells possess within the plasma membrane a variety of proteins involved in the reception, transduction and amplification of extra-cellular signals that mediate transmembrane processes.

Architecture of Plasma Membrane Hormone Receptor-Effector Systems

The hormonally responsive adenylate cyclase system is an example of a system subject to complex regulation that undergoes shifts in equilibria of binding of components to one another and to elements

Dual regulation of adenylate cyclase. A signal transduction mechanism of membrane receptors

The hormone-sensitive adenylate cyclase is a multi-component system embedded in the lipid bilayer of the plasma membrane and serves as a signal transduction system for various membrane receptors and its regulation will be briefly reviewed.

G proteins and the mechanism of action of hormones, neurotransmitters, and autocrine and paracrine regulatory factors.

This work discusses the features of signal transduction by G proteins, which provide for amplification, reversal of action, and continued monitoring of incoming signals.

Inhibitory coupling of hormone and neurotransmitter receptors to adenylate cyclase.

Several lines of evidence are presented suggesting that the guanine nucleotide-dependent component apparently involved in adenylate cyclase inhibition and apparently exhibiting GTPase activity is at least partially different from that involved in advertisement cyclase stimulation by hormones.

Receptor Mediated Activation of Phospholipase A2: Arachidonic Acid and its Metabolites as Second Messengers

GTP binding proteins, called G or N proteins, are involved in receptor-mediated signal transduction in cells and are shown to cause the activation or inhibition, respectively, of adenylate cyclase.
...

References

SHOWING 1-10 OF 187 REFERENCES

Reduction of GTP activation of adenylate cyclase system by its coupling to hormone receptor.

It is proposed that changes in the characteristics of the adenylate cyclase system reflect an interaction between the beta-adrenergic receptor and the nucleotide regulatory component and that this interaction represents, at least in part, the process of coupling.

Influence of cholera toxin on the regulation of adenylate cyclase by GTP.

ADP-ribosylation of membrane proteins catalyzed by cholera toxin: basis of the activation of adenylate cyclase.

  • D. GillR. Meren
  • Biology
    Proceedings of the National Academy of Sciences of the United States of America
  • 1978
Evidence is presented that suggests that the most readily modified membrane protein is the adenylate cyclase-associated GTP-binding protein, which is stimulated by guanine nucleotides in cholera toxin fragment A1.

Determination of the turn-off reaction for the hormone-activated adenylate cyclase.

The finding of similar rate constants in the various preparations indicates that GTP hydrolysis at the regulatory site is a general mechanism for terminating the activation of adenylate cyclase.

The fat cell adenylate cyclase system. Characterization and manipulation of its bimodal regulation by GTP.

The persistence of the bimodal response under a variety of assay conditions suggests a central role for GTP in mediating both activation and inhibition of adenylate cyclase by agents which act through cell surface receptors.
...