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GRK5  -  G protein-coupled receptor kinase 5

Bos taurus

 
 
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High impact information on GPRK5

  • In vivo interaction of GRK and tubulin was suggested by the following: (i) co-purification of betaARK with tubulin from brain tissue; (ii) co-immunoprecipitation of betaARK and tubulin from COS-1 cells; and (iii) co-localization of betaARK and GRK5 with microtubule structures in COS-1 cells [1].
  • Intact cell studies reveal that GRK5 is also phosphorylated when transiently expressed in COS-1 cells following treatment with the PKC activator, phorbol 12-myristate 13-acetate [2].
  • In this study we demonstrate that phosphatidylinositol 4, 5-bisphosphate (PIP2) enhances GRK5-mediated beta-adrenergic receptor (betaAR) phosphorylation by directly interacting with this enzyme and facilitating its membrane association [3].
  • The lipid binding site of GRK5 exhibits a high degree of specificity and appears to reside in the amino terminus of this enzyme [3].
  • GRK5-mediated phosphorylation of a soluble peptide substrate is unaffected by PIP2, suggesting that the PIP2-enhanced receptor kinase activity arises as a consequence of this membrane localization [3].
 

Biological context of GPRK5

 

Anatomical context of GPRK5

 

Associations of GPRK5 with chemical compounds

  • Mutation of six basic residues at positions 22, 23, 24, 26, 28, and 29 of GRK5 ablates the ability of this kinase to bind PIP2 [3].
 

Enzymatic interactions of GPRK5

References

  1. Binding and phosphorylation of tubulin by G protein-coupled receptor kinases. Carman, C.V., Som, T., Kim, C.M., Benovic, J.L. J. Biol. Chem. (1998) [Pubmed]
  2. Regulation of the G protein-coupled receptor kinase GRK5 by protein kinase C. Pronin, A.N., Benovic, J.L. J. Biol. Chem. (1997) [Pubmed]
  3. Phosphatidylinositol 4,5-bisphosphate (PIP2)-enhanced G protein-coupled receptor kinase (GRK) activity. Location, structure, and regulation of the PIP2 binding site distinguishes the GRK subfamilies. Pitcher, J.A., Fredericks, Z.L., Stone, W.C., Premont, R.T., Stoffel, R.H., Koch, W.J., Lefkowitz, R.J. J. Biol. Chem. (1996) [Pubmed]
  4. Identification, purification, and characterization of GRK5, a member of the family of G protein-coupled receptor kinases. Premont, R.T., Koch, W.J., Inglese, J., Lefkowitz, R.J. J. Biol. Chem. (1994) [Pubmed]
  5. Characterization of the G protein-coupled receptor kinase GRK4. Identification of four splice variants. Premont, R.T., Macrae, A.D., Stoffel, R.H., Chung, N., Pitcher, J.A., Ambrose, C., Inglese, J., MacDonald, M.E., Lefkowitz, R.J. J. Biol. Chem. (1996) [Pubmed]
 
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