PUBLICATION

R9AP, a membrane anchor for the photoreceptor GTPase accelerating protein, RGS9-1c

Authors
Hu, G. and Wensel, T.G.
ID
ZDB-PUB-020820-14
Date
2002
Source
Proceedings of the National Academy of Sciences of the United States of America   99(15): 9755-9760 (Journal)
Registered Authors
Keywords
none
MeSH Terms
  • Adaptor Proteins, Signal Transducing
  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cattle
  • Cell Membrane/physiology
  • Cloning, Molecular
  • DNA, Complementary
  • GTP Phosphohydrolases/metabolism*
  • Membrane Proteins/chemistry
  • Membrane Proteins/genetics
  • Membrane Proteins/metabolism*
  • Molecular Sequence Data
  • Molecular Weight
  • Peptide Fragments/chemistry
  • Photoreceptor Cells, Vertebrate/physiology*
  • Protein Structure, Secondary
  • RGS Proteins/metabolism*
  • Rabbits
  • Recombinant Proteins/chemistry
  • Recombinant Proteins/isolation & purification
  • Recombinant Proteins/metabolism
  • Rod Cell Outer Segment/metabolism*
PubMed
12119397 Full text @ Proc. Natl. Acad. Sci. USA
Abstract
The regulator of G protein signaling (RGS)-9-1.G(beta5) complex forms the GTPase accelerating protein for G(alphat) in vertebrate photoreceptors. Although the complex is soluble when expressed in vitro, extraction of the endogenous protein from membranes requires detergents. The detergent extracts contain a complex of RGS9-1, G(beta5), G(alphat), and a 25-kDa phosphoprotein, R9AP (RGS9-1-Anchor Protein). R9AP is encoded by one intronless gene in both human and mouse. Full or partial cDNA or genomic clones were obtained from mice, cattle, human, zebrafish, and Xenopus laevis. R9AP mRNA was detected only in the retina, and the protein only in photoreceptors. R9AP binds to the N-terminal domain of RGS9-1, and anchors it to the disk membrane via a C-terminal transmembrane helix.
Genes / Markers
Figures
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Antibodies
Orthology
Engineered Foreign Genes
Mapping