RGS9-G beta 5 substrate selectivity in photoreceptors. Opposing effects of constituent domains yield high affinity of RGS interaction with the G protein-effector complex.
Journal Article (Journal Article)
RGS proteins regulate the duration of G protein signaling by increasing the rate of GTP hydrolysis on G protein alpha subunits. The complex of RGS9 with type 5 G protein beta subunit (G beta 5) is abundant in photoreceptors, where it stimulates the GTPase activity of transducin. An important functional feature of RGS9-G beta 5 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-G beta 5 make opposite contributions toward this selectivity. G beta 5 bound to the G protein gamma 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.
Full Text
Duke Authors
Cited Authors
- Skiba, NP; Martemyanov, KA; Elfenbein, A; Hopp, JA; Bohm, A; Simonds, WF; Arshavsky, VY
Published Date
- October 5, 2001
Published In
Volume / Issue
- 276 / 40
Start / End Page
- 37365 - 37372
PubMed ID
- 11495924
Pubmed Central ID
- 11495924
International Standard Serial Number (ISSN)
- 0021-9258
Digital Object Identifier (DOI)
- 10.1074/jbc.M106431200
Language
- eng
Conference Location
- United States