Blake A D, Mumford R A, Strout H V, Slater E E, Strader C D
Biochem Biophys Res Commun. 1987 Aug 31;147(1):168-73. 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.
在某些细胞系统中，β-肾上腺素能受体的脱敏作用与受体磷酸化相关。多种激酶参与了这些磷酸化过程，包括环磷酸腺苷（cAMP）依赖性蛋白激酶和蛋白激酶C。在本研究中，我们利用从哺乳动物β-肾上腺素能受体克隆获得的蛋白质序列信息，制备了与受体区域相对应的合成肽，这些区域预计在体内可作为这些激酶的可能底物。发现其中两种源自受体的肽可作为这些蛋白激酶的底物。对应于β受体第257 - 264位氨基酸的肽是cAMP依赖性蛋白激酶的首选底物，而蛋白激酶C对对应于β-肾上腺素能受体第341 - 351位残基的肽的磷酸化表现出明显偏好。
