Scripps VIVO scripps research logo

  • Index
  • Log in
  • Home
  • People
  • Organizations
  • Research
  • Events
Search form
As of April 1st VIVO Scientific Profiles will no longer updated for faculty, and the link to VIVO will be removed from the library website. Faculty profile pages will continue to be updated via Interfolio. VIVO will continue being used behind the scenes to update graduate student profiles. Please contact helplib@scripps.edu if you have questions.
How to download citations from VIVO | Alternative profile options

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

Academic Article
uri icon
  • Overview
  • Identity
  • Additional Document Info
  • View All
scroll to property group menus

Overview

authors

  • Skiba, N. P.
  • Martemyanov, Kirill
  • Elfenbein, A.
  • Hopp, J. A.
  • Bohm, A.
  • Simonds, W. F.
  • Arshavsky, V. Y.

publication date

  • October 2001

journal

  • Journal of Biological Chemistry  Journal

abstract

  • 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.

subject areas

  • 3',5'-Cyclic-GMP Phosphodiesterases
  • Animals
  • Catalysis
  • Cattle
  • Cyclic Nucleotide Phosphodiesterases, Type 6
  • GTP-Binding Protein beta Subunits
  • Heterotrimeric GTP-Binding Proteins
  • Kinetics
  • Photoreceptor Cells
  • Protein Structure, Tertiary
  • RGS Proteins
  • Substrate Specificity
  • Transducin
scroll to property group menus

Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.M106431200

PubMed ID

  • 11495924
scroll to property group menus

Additional Document Info

start page

  • 37365

end page

  • 37372

volume

  • 276

issue

  • 40

©2022 The Scripps Research Institute | Terms of Use | Powered by VIVO

  • About
  • Contact Us
  • Support