Synthetic segments of the mammalian beta AR are preferentially recognized by cAMP-dependent protein kinase and protein kinase C.
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.
Blake
A D
AD
Mumford
R A
RA
Strout
H V
HV
Slater
E E
EE
Strader
C D
CD
D000595:Amino Acid Sequence; D000818:Animals; D006224:Cricetinae; D007700:Kinetics; D009842:Oligopeptides / Q000138:chemical synthesis / Q000378:metabolism*; D010766:Phosphorylation; D011493:Protein Kinase C / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism*; D011943:Receptors, Adrenergic, beta / Q000378:metabolism*; D012694:Serine / Q000378:metabolism; D013329:Structure-Activity Relationship
D009842:Oligopeptides; D011943:Receptors, Adrenergic, beta; D012694:Serine; D011494:Protein Kinases; D011493:Protein Kinase C