Dynamics of G protein effector interactions and their impact on timing and sensitivity of G protein-mediated signal transduction
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Updated: Apr 10, 2026

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
Published on: February 20, 2018
Eva-Lisa Bodmann1, Valerie Wolters1, Moritz Bünemann1
1Institute for Pharmacology and Clinical Pharmacy, Faculty of Pharmacy, Philipps-University Marburg, Karl-von-Frisch-Str. 1, 35043 Marburg, Germany.
Abstract:
G protein coupled receptors regulate numerous cellular functions primarily via coupling to heterotrimeric G proteins and subsequent regulation of effector proteins such as ion channels, enzymes or GTP exchange factors for small G proteins. The dynamics of interactions between G protein subunits and effectors have been difficult to study particularly in a cellular context. The introduction of Förster resonance energy transfer methods into the field of GPCR research led to interesting insights into the temporal patterns of interactions between G protein subunits and their effectors. In this review we specifically focus on the interaction of Gαi subunits with adenylyl cyclases and of Gαq subunits with p63RhoGEF or G protein coupled receptor kinases type 2. Comparing the dynamics of these interactions revealed remarkable differences between different G protein effectors regarding the ability to be modulated by members of the regulator of G protein signalling protein family as well as the sensitivity towards receptor activation.
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