Abstract
Phosphorylation is a fundamental regulatory mechanism employed by many G protein-coupled receptors (GPCRs). There are presently at least 26 G protein-coupled receptor subtypes that have been demonstrated to undergo agonist-dependent phosphorylation (1). In fact, of the receptor subtypes studied, only three—namely the α2C4-adrenoceptor (2), β3-adrenoceptor (3), and the gonadotrophin-releasing hormone receptor (4—are thought not to undergo agonist-sensitive phosphorylation. It seems likely, therefore, that most GPCRs will undergo some form of phosphorylation, and with there being over 100 known members of this gene superfamily, interest in identification of receptor phosphorylation events will remain high.
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References
Tobin A. B. (1996) Receptor-specific kinases in the regulation of phospholipaseC-coupled receptors, in The Phospholipase C pathway Its Regulation and Desensitisatzon (Tobin A. B., ed.), Landes, Austin, Texas.
Kurose H. and Lefkowitz R. J. (1994) Differential desensitisatlon and phosphorylation of three cloned and transfected az-adrenergtc receptor subtypes. J. Bzol Chem 269, 10,093–l0,099.
Liggett S. B. and Lefkowrtz R. J (1994) Adrenerglc receptor-coupled adenylylcyclase systems: regulation of receptor function by phosphorylation, sequestration and down-regulation, in Regulation of Cellular Signal Transduction Pathways by Desensitrsation and Amphjkatron (Sibley D. R and Houslay M D., eds.), John Wiley, Chichester.
McArdle C. A., Forrest-Owen W, Willars G, Davidson J, Poch A., and Kratzmeier M. (1995) Desensitisation of gonadotropin-releasing hormone action in the gonadotrope derived αT3-1 cell line. Endocrrnology 136, 4864–4871.
Stadel J. M., Nambt P., Shorr R. G. L., Sawyer D. F., Caron M. G., and Lefkowitz R. J. (1983) Catecholamme-induced desensitisatlon of turkey erythrocyte adenylate cyclase is associated with phosphorylatlon of the β-adrenergic receptor. Proc. Natl. Acad. Sci. USA 80, 3173–3177.
Benovrc J. F., Mayor F., Staniszewski C., Letkowttz R. J., and Caron M. G. (1987) Purification and characterisation of β-adrenergic receptor kinase. J Biol Chem. 262, 9026–9032.
Kwatra M. M. and Hosey M. M (1986) Phosphorylation of the cardiac muscarinic receptor in intact chick heart and its regulation by a muscarinic agonist J Biol. Chem. 261, 12,429–12,432.
Leeb-Lundberg L. M., Cotecchia S., DeBlasi A., Caron M. G., and Lefkownz R. J. (1987) Regulation of adrenergic receptor function by phosphorylatron. J. Biol. Chem. 262, 3098–3105.
Tobin A. B. and Nahorskt S. R (1993) Rapid agonist mediated phosphorylation of m3-muscarinic receptors revealed by immunoprecipitatron. J. Biol. Chem. 268, 9817–9823.
Tobin A. B., Keys B., and Nahorski S. R. (1993). Phosphorylation of a phosphoinositidase C-linked muscarinic receptor by a novel kmase distinct from β-adrenergic receptor kinase. FEBSLett. 335, 353–357.
Palmer T. M., Benovic J. L., and Stiles G L. (1995) Agonist-dependent phosphorylation and desensitisation of the rat A3-adenosme receptor. J. Biol Chem. 270, 29,607–29,613.
Tobin A. B., Keys B., and Nahorski S. R. (1996) Purification and characterisation of a novel receptor-specific kinase that phosphorylates a PLC-coupled muscarinic receptor. J Biol Chem 271, 3907–3916.
Prossnitz E. R., Kim C. M., Benovic B. L., and Ye R. D. (1995) Phosphorylation of the N-formyl peptide receptor carboxyl terminus by the G protein coupled receptor kinase, GRK2. J. Biol Chem 270, 1130–1137.
Harlow E. and Lane D. (1984) Antrbodies: A Laboratory Manual. Cold Spring Harbor Laboratory, Cold Spring Harbor, NY.
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Tobin, A.G. (1997). Protocols Employed in the Investigation of G Protein-Coupled Receptor Phosphorylation. In: Challiss, R.A.J. (eds) Receptor Signal Transduction Protocols. Methods in Molecular Biology™, vol 83. Humana Press. https://doi.org/10.1385/0-89603-495-X:227
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DOI: https://doi.org/10.1385/0-89603-495-X:227
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