Background: Intracellular trafficking of RGS proteins is an important determinant of their function as G-protein inhibitors. Results: Amino-terminal cysteine residues in RGS4 confer previously uncharacterized localization and trafficking activities. Conclusion: Cys-12 is required for plasma membrane targeting, whereas Cys-2 is required for localization to endosomal pools. Significance: Understanding the mechanisms governing cellular distribution of RGS4 may lead to novel strategies for regulation of its function.
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