Localization of G_iα proteins in the centrosomes and at the midbody: implication for their role in cell division

At the plasma membrane, heterotrimeric G proteins act as molecular switches to relay signals from G protein–coupled receptors; however, G_α subunits also have receptor-independent functions at intracellular sites. Regulator of G protein signaling (RGS) 14, which enhances the intrinsic GTPase activity of G_iα proteins, localizes in centrosomes, which suggests the coexpression of G_iα. We show expression of G_iα1, G_iα2, and G_iα3 in the centrosomes and at the midbody. Fluorescence resonance energy transfer analysis confirms a direct interaction between RGS14 and G_iα1 in centrosomes. Expression of GTPase-deficient G_iα1 results in defective cytokinesis, whereas that of wild-type or GTPase-deficient G_iα3 causes prolonged mitosis. Cells treated with pertussis toxin, with reduced expression of G_iα1, G_iα2, and G_iα3 or with decreased expression of RGS14 also exhibit cytokinesis defects. These results suggest that G_iα proteins and their regulators at these sites may play essential roles during mammalian cell division.