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Updated: Aug 23, 2026

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
Published on: February 20, 2018
Translating G protein subunit diversity into functional specificity
Janet D Robishaw1, Catherine H Berlot
1100 N. Academy Ave, Weis Center for Research, Geisinger Clinic, Danville, PA 17822-2614, USA. jrobishaw@geisinger.edu
Historically, it has been assumed that the functional roles of G proteins in receptor recognition and effector regulation are specified by their diverse alpha subunits. However, the discovery of similarly diverse betagamma subunits that participate in both of these functional processes has called this assumption into question; recent work suggests that G proteins function as heterotrimers whose roles in particular receptor signaling pathways are determined by their specific alphabetagamma subunit combinations. Although much remains to be learned, the assembly of specific alphabetagamma subunit combinations seems to involve both structural and spatial factors.
Historically, it has been assumed that the functional roles of G proteins in receptor recognition and effector regulation are specified by their diverse alpha subunits. However, the discovery of similarly diverse betagamma subunits that participate in both of these functional processes has called this assumption into question; recent work suggests that G proteins function as heterotrimers whose roles in particular receptor signaling pathways are determined by their specific alphabetagamma subunit combinations. Although much remains to be learned, the assembly of specific alphabetagamma subunit combinations seems to involve both structural and spatial factors.
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