The regulators of G protein signaling (RGS proteins) bind directly to G protein alpha (Gα) subunits in brain and other tissues to determine the strength, duration, and fidelity of neurotransmitter receptor signaling. A recent study shows, quite unexpectedly, that one class of RGS proteins [the R7 subfamily bound to Gβ5 (R7-Gβ5)] shuttles between the plasma membrane and the nucleus with assistance from a novel shuttle protein, R7BP. R7BP binds directly to R7-Gβ5 and the protein complex is tethered to the plasma membrane by addition of a lipid, palmitate, on R7BP. Removal of palmitate results in the translocation of the R7BP–R7-Gβ5 complex to the nucleus, presumably for nontraditional signaling functions. These findings suggest an entirely novel mechanism for regulating neurotransmitter signaling. That is, R7BP transduces signals directly from receptors and G proteins at the plasma membrane to the nucleus, and this plasma membrane–nuclear shuttling is controlled by reversible palmitoylation of R7BP.


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      NSDL,NSDL_SetSpec_BEN,oai:nsdl.org:2200/20080618220007119T,signal transduction,heterotrimeric G proteins,palmitoylation,Life Science



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