Specificity of G protein-RGS protein recognition is regulated by affinity adapters.

Journal Article

RGS proteins regulate the duration of cell signaling by modulating the lifetime of activated G proteins. The specificity of RGS-G protein mutual recognition is critical for meeting unique timing requirements of numerous G protein-mediated pathways. Our study of two splice isoforms of RGS9 expressed in different types of neurons revealed a novel mechanism whereby this specificity is determined by specialized protein domains or subunits acting as affinity adapters. The long RGS9 isoform contains a C-terminal domain that provides high-affinity interaction with its target G protein. The lack of this domain in the short RGS9 isoform is compensated by the action of a G protein effector subunit that is structurally similar to this C-terminal domain. This allows the short isoform to specifically target the complex between the G protein and its effector. Thus, the specific timing needs of different signaling pathways can be accommodated by affinity adapters positioned at various pathway components.

Full Text

Duke Authors

Cited Authors

  • Martemyanov, KA; Hopp, JA; Arshavsky, VY

Published Date

  • June 19, 2003

Published In

Volume / Issue

  • 38 / 6

Start / End Page

  • 857 - 862

PubMed ID

  • 12818172

International Standard Serial Number (ISSN)

  • 0896-6273

Language

  • eng

Conference Location

  • United States