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Molecular Pharmacology Fast Forward
First published on July 16, 2007; DOI: 10.1124/mol.107.040055


0026-895X/07/7204-810-811$20.00
Mol Pharmacol 72:810-811, 2007

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Perspective

Illuminating Gβ5 Signaling

Corinne E. Zeller, and Henrik G. Dohlman

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 {gamma} 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{gamma} subunits as well as regulator of G protein signaling (RGS) proteins that contain a G{gamma}-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{gamma} pairings.


Received July 16, 2007; accepted July 16, 2007

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:

Live Cell Analysis of G Protein beta5 Complex Formation, Function, and Targeting
Evan A. Yost, Stacy M. Mervine, Jonathan L. Sabo, Thomas R. Hynes, and Catherine H. Berlot
MolPharm 2007 72: 812-825. [Abstract] [Full Text]  






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