RT Journal Article SR Electronic T1 Illuminating Gβ5 Signaling JF Molecular Pharmacology JO Mol Pharmacol FD American Society for Pharmacology and Experimental Therapeutics SP 810 OP 811 DO 10.1124/mol.107.040055 VO 72 IS 4 A1 Corinne E. Zeller A1 Henrik G. Dohlman YR 2007 UL http://molpharm.aspetjournals.org/content/72/4/810.abstract AB G proteins are key intermediates in cellular signaling and act in response to a variety of extracellular stimuli. The prevailing paradigm is that G protein subunits form a heterotrimeric complex and function principally at the plasma membrane. However, there is growing evidence for localization at, and signaling by, G proteins at intracellular compartments. Moreover, different cellular pools of G proteins may be composed of distinct subunit subtypes, including some binding partners that function in the place of G protein γ subunits. An article in this issue of Molecular Pharmacology (Yost et al., p. 812) describes the use of an innovative fluorescent cell imaging technique to study interactions of the G protein β5 subunit with a panel of Gγ subunits as well as regulator of G protein signaling (RGS) proteins that contain a Gγ-like subdomain. The approach used here provides a new strategy to elucidate the spatial and temporal properties of G proteins, including a growing number of atypical Gβγ pairings. The American Society for Pharmacology and Experimental Therapeutics