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Updated: Aug 17, 2026

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators
Published on: February 20, 2018
Two G12 family G proteins, G alpha12 and G alpha13, show different subcellular localization
Junya Yamazaki1, Hironori Katoh, Yoshiaki Yamaguchi
1Laboratory of Molecular Neurobiology, Graduate School of Biostudies, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Abstract:
The G alpha subunits of the G12 family of heterotrimeric G proteins, G alpha12 and G alpha13, are closely related in sequences and some effectors, but they often act through different pathways or bind to different proteins. We have examined subcellular distribution of these two G proteins and found that endogenous G alpha12 and G alpha13 localize in membrane and cytoplasmic fractions, respectively. Exogenously expressed G alpha12 and G alpha13 also localize in membrane and cytoplasmic fractions, respectively, in COS-7 cells. Stimulation of lysophosphatidic acid receptor coupled to G alpha13 markedly promotes the translocation of G alpha13 from cytoplasm to membrane. This different localization of G alpha12 and G alpha13 may explain some of the nonoverlapping actions of G alpha12 and G alpha13.
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