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Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, North Carolina
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
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 G
subunits as well as regulator of G protein signaling (RGS) proteins that contain a G
-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 Gβ
pairings.
Address correspondence to: Henrik G. Dohlman, Department of Biochemistry & Biophysics, University of North Carolina at Chapel Hill, 116 Manning Dr., CB 7260, Chapel Hill, NC 27599. E-mail: henrik_dohlman{at}med.unc.edu
Related articles in MolPharm:
5 Complex Formation, Function, and Targeting