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.

Published

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