Synthetic segments of the mammalian βAR are preferentially recognized by cAMP-dependent protein kinase and protein kinase C

• Published in: Biochemical and biophysical research communications Vol. 147; no. 1; pp. 168 - 173
• Main Authors: Blake, Allan D., Mumford, Richard A., Vincent Strout, H., Slater, Eve E., Strader, Catherine D.
• Format: Journal Article
• Language: English
• Published: San Diego, CA Elsevier Inc 31.08.1987; Elsevier
• Subjects: Amino Acid Sequence; Animals; Applied sciences; Cricetinae; Exact sciences and technology; Kinetics; Oligopeptides - chemical synthesis; Oligopeptides - metabolism; Other techniques and industries; Phosphorylation; protein kinase; protein kinase C; Protein Kinase C - metabolism; Protein Kinases - metabolism; receptors; Receptors, Adrenergic, beta - metabolism; Serine - metabolism; Structure-Activity Relationship; PKC; TPA; βAR; PKA
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1016/S0006-291X(87)80102-X

Desensitization of the beta-adrenergic receptor has been correlated in some cell systems with receptor phosphorylation. Various kinases have been implicated in these phosphorylation processes, including both cAMP-dependent protein kinase and protein kinase C. In the present study, we have utilized the protein sequence information obtained from the cloning of the mammalian beta-adrenergic receptor to prepare synthetic peptides corresponding to regions of the receptor which would be predicted to act as possible substrates for these kinases in vivo. Two of these receptor-derived peptides were found to serve as substrates for these protein kinases. A peptide corresponding to amino acids 257–264 of the beta-receptor is the preferred substrate for the cAMP-dependent protein kinase, while protein kinase C showed a marked preference for phosphorylation of a peptide corresponding to residues 341–351 of the beta-adrenergic receptor.