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. 2017 Mar 1;2(1):48–60. doi: 10.1089/can.2016.0037

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© Mikkel Søes Ibsen et al. 2017; Published by Mary Ann Liebert, Inc.

This Open Access article is distributed under the terms of the Creative Commons License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited.

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FIG. 1. — Biased agonist 1 or 2 binds to the seven-transmembrane cannabinoid receptor 1. Structurally different ligands will induce diverse conformations of the receptor, which may then favor one of the possible signaling pathways over others. In this diagram, agonist 1 is biased toward the activation of the Gα_i/o heterotrimer over β-arrestin-1, while agonist 2 favorably activates β-arrestin-1. Activation of Gα_i/o prompts the release of the Gβγ subunit, which inhibits voltage-dependent calcium channels (I_Ca) and activates GIRK. The Gα_i/o subunit inhibits AC, which stimulates the phosphorylation and early activation of ERK1/2. The activation of β-arrestin-1 conversely induces late activation of ERK1/2. AC, adenylyl cyclase; ERK1/2, extracellular signal-regulated kinase 1 or 2; GIRK, G protein-gated inwardly rectifying potassium channels.