GRK2 antibody

Source

Rabbit

Reactivity

Human;Mouse;Rat

Background

G protein-coupled receptor kinase 2, also known as beta-adrenergic receptor kinase 1, is a member of the GRK family, which phosphorylates the activated form of G protein-coupled receptors and initiates the desensitization process of GPCR. GRK2 kinase activity and cellular localization are tightly regulated by interactions with activated receptors, G-beta and G-gamma subunits, adaptor proteins, phospholipids, caveolin, and calmodulin, as well as by phosphorylation. Protein kinase C phosphorylation enhances GRK2 activity by promoting its membrane localization and by abolishing the inhibitory association of calmodulin. Protein kinase A phosphorylates GRK2 at Ser685, facilitating the association of GRK2 with a beta-adrenergic receptor. Erk inhibits GRK2 activity via phosphorylation at Ser670. Src phosphorylates GRK2 at multiple tyrosine residues, which activates GRK2 activity and promotes GRK2 degradation.

References

[1] Pitcher, J. A. et al. (1998) Annu. Rev. Biochem. 67, 653-692.
[2] Winstel, R. et al. (1996) Proc. Natl. Acad. Sci. USA 93, 2105-2109.
[3] Krasel, C. et al. (2001) J. Biol. Chem. 276, 1911-1915.
[4] Cong, M. et al. (2001) J. Biol. Chem. 276, 15192-15199.
[5] Pitcher, J. A. et al. (1999) J. Biol. Chem. 274, 34531-34534.
[6] Sarnago, S. et al. (1999) J. Biol. Chem. 274, 34411-34416.
[7] Penela, P. et al. (2001) EMBO J. 20, 5129-5138.