Skip to main content

Identification, purification, and characterization of GRK5, a member of the family of G protein-coupled receptor kinases.

Publication ,  Journal Article
Premont, RT; Koch, WJ; Inglese, J; Lefkowitz, RJ
Published in: J Biol Chem
March 4, 1994

A novel member of the family of G protein-coupled receptor kinases (GRKs), named GRK5, has been cloned from bovine taste epithelium. The cDNA sequence predicts a 590-amino acid protein with high overall similarity to rhodopsin kinase. GRK5 mRNA is found most abundantly in lung, heart, retina, and lingual epithelium, but is expressed very little in brain, liver, kidney, or testis. GRK5 expressed in Sf9 cells was purified to apparent homogeneity. GRK5 major autophosphorylation sites were mapped to Ser484 and Thr485. Purified GRK5 phosphorylates rhodopsin in a light-dependent manner and beta 2-adrenergic receptor in an agonist-dependent manner and phosphorylates the C-terminal tail regions of both receptor proteins. GRK5 possesses neither a CAAX motif specifying protein prenylation like rhodopsin kinase nor similarity to the G protein beta gamma-subunit binding domain of beta-adrenergic receptor kinases. GRK5 phosphorylation of rhodopsin or beta 2-adrenergic receptor is not stimulated by G protein beta gamma-subunits. The GRK5 protein does not undergo agonist-dependent translocation from cytosol to membranes as do beta-adrenergic receptor kinase and rhodopsin kinase, but rather appears to associate with membranes constitutively. GRK5 thus appears functionally similar to other characterized GRKs, but has distinct regulatory properties which may be important for its cellular function.

Duke Scholars

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

March 4, 1994

Volume

269

Issue

9

Start / End Page

6832 / 6841

Location

United States

Related Subject Headings

  • Threonine
  • Taste
  • Serine
  • Rhodopsin
  • Restriction Mapping
  • Receptor Protein-Tyrosine Kinases
  • RNA, Messenger
  • Protein Serine-Threonine Kinases
  • Polymerase Chain Reaction
  • Phosphorylation
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Premont, R. T., Koch, W. J., Inglese, J., & Lefkowitz, R. J. (1994). Identification, purification, and characterization of GRK5, a member of the family of G protein-coupled receptor kinases. J Biol Chem, 269(9), 6832–6841.
Premont, R. T., W. J. Koch, J. Inglese, and R. J. Lefkowitz. “Identification, purification, and characterization of GRK5, a member of the family of G protein-coupled receptor kinases.J Biol Chem 269, no. 9 (March 4, 1994): 6832–41.
Premont RT, Koch WJ, Inglese J, Lefkowitz RJ. Identification, purification, and characterization of GRK5, a member of the family of G protein-coupled receptor kinases. J Biol Chem. 1994 Mar 4;269(9):6832–41.
Premont, R. T., et al. “Identification, purification, and characterization of GRK5, a member of the family of G protein-coupled receptor kinases.J Biol Chem, vol. 269, no. 9, Mar. 1994, pp. 6832–41.
Premont RT, Koch WJ, Inglese J, Lefkowitz RJ. Identification, purification, and characterization of GRK5, a member of the family of G protein-coupled receptor kinases. J Biol Chem. 1994 Mar 4;269(9):6832–6841.

Published In

J Biol Chem

ISSN

0021-9258

Publication Date

March 4, 1994

Volume

269

Issue

9

Start / End Page

6832 / 6841

Location

United States

Related Subject Headings

  • Threonine
  • Taste
  • Serine
  • Rhodopsin
  • Restriction Mapping
  • Receptor Protein-Tyrosine Kinases
  • RNA, Messenger
  • Protein Serine-Threonine Kinases
  • Polymerase Chain Reaction
  • Phosphorylation