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Cell Signal ; 16(6): 711-21, 2004 Jun.
Article in English | MEDLINE | ID: mdl-15093612

ABSTRACT

Regulator of G protein signaling (RGS) proteins function as GTPase accelerating proteins (GAP) for Galpha subunits, attenuating G-protein-coupled receptor signal transduction. The present study tested the ability of members of different subfamilies of RGS proteins to modulate both G-protein-dependent and -independent signaling in mammalian cells. RGS4, RGS10, and RGSZ1 significantly attenuated Galphai-mediated signaling by 5-HT1A, but not by dopamine D2, receptor-expressing cells. Additionally, RGS4 and RGS10 significantly inhibited forskolin-stimulated cAMP production in both cell lines. In contrast, RGS2, RGS7, and RGSZ1 had no effect on forskolin-stimulated cAMP production in these cells. RGS2 and RGS7 significantly decreased Galphaq-mediated signaling by 5-HT2A receptors, confirming that the RGS4 and RGS10 effects on forskolin-stimulated cAMP production were specific, and not simply due to overexpression. Interestingly, similar expression levels of RGS4 protein resulted in greater inhibition of G-protein-independent cAMP production compared to G-protein-dependent GAP activity. Our results suggest specificity and selectivity of RGS proteins on G-protein-dependent and -independent signaling in mammalian cells.


Subject(s)
GTP-Binding Proteins/metabolism , RGS Proteins/metabolism , Receptors, Dopamine D2/metabolism , Receptors, Serotonin, 5-HT1/metabolism , Receptors, Serotonin, 5-HT2/metabolism , Adenylyl Cyclases/drug effects , Animals , Colforsin/pharmacology , Cricetinae , Cricetulus , Cyclic AMP/metabolism , Enzyme Activation/drug effects , Signal Transduction/physiology
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