RGS proteins regulate the duration of G protein signaling by increasing the rate of GTP hydrolysis on G protein α subunits. The complex of RGS9 with type 5 G protein β subunit (Gβ5) is abundant in photoreceptors, where it stimulates the GTPase activity of transducin. An important functional feature of RGS9-Gβ5 is its ability to activate transducin GTPase much more efficiently after transducin binds to its effector, cGMP phosphodiesterase. Here we show that different domains of RGS9-Gβ5 make opposite contributions toward this selectivity. Gβ5 bound to the G protein γ subunit-like domain of RGS9 acts to reduce RGS9 affinity for transducin, whereas other structures restore this affinity specifically for the transducin-phosphodiesterase complex. We suggest that this mechanism may serve as a general principle conferring specificity of RGS protein action.
RGS9-Gβ5 Substrate Selectivity in Photoreceptors
N. Skiba,K. Martemyanov,A. Elfenbein,J. A. Hopp,A. Bohm,W. Simonds,V. Arshavsky
Published 2001 in Journal of Biological Chemistry
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- Publication year
2001
- Venue
Journal of Biological Chemistry
- Publication date
2001-10-05
- Fields of study
Biology
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