Principles
Agonist-receptor efficacy II: agonist trafficking of receptor signals

https://doi.org/10.1016/S0165-6147(00)89032-XGet rights and content

Abstract

There is evidence to suggest that receptors with seven transmembrane domains can exist in G protein-activating conformations. It is not known how many activated receptor forms exist for each receptor. Furthermore, if there are multiple forms, does the chemical structure of the agonist determine which form dominates, and therefore, which response pathway is activated? This latter scheme is referred to as agonist-receptor trafficking, and is discussed in this, the second of two articles by Terry Kenakin. One way to approach these questions is to study receptors that couple to more than one G protein and, in essence, to try to allow the G protein to indicate the receptor state.

References (18)

  • T. Kenakin

    Trends Pharmacol. Sci.

    (1995)
  • T.P. Kenakin

    Life Sci.

    (1988)
  • C.A. Maggi et al.

    Eur. J. Pharmacol.

    (1993)
  • T.P. Kenakin

    Trends Pharmacol. Sci.

    (1994)
  • J-L. Bascands et al.

    Mol. Pharmacol.

    (1993)
  • T. Costa et al.

    Mol. Pharmacol.

    (1988)
  • R.R. Neubig

    FASEB J.

    (1994)
  • D.F. Matesic et al.

    Mol. Pharmacol.

    (1991)
  • M.G. Eason et al.

    Mol. Pharmacol.

    (1994)
There are more references available in the full text version of this article.

Cited by (595)

  • Commentary on the development of receptor theory by John Parascandola

    2023, Standardizing Pharmacology: Assays and Hormones Discoveries in Pharmacology: Volume 2
  • β-Adrenoceptor Antagonists

    2022, Comprehensive Pharmacology
  • Agonism and Biased Signaling

    2022, Comprehensive Pharmacology
View all citing articles on Scopus
View full text