Differential phosphorylation of ribosomal protein S6 in isolated rat hepatocytes after incubation with insulin and glucagon

FEBS Letters

Holland, Ross²  Caudwell, Barry²  Cohen, Philip²  Wettenhall, Richard E.H.¹ 

[1] Department of Biochemistry, La Trobe University, Bundoora, VIC 3083, Australia;Departmentof Biochemistry, Medical Sciences Institute, University of Dundee, Dundee DD1 4HN, Scotland

关键词: Ribosomes;    Glucagon;    Insulin;    Cyclic AMP;    Protein synthesis;    Hepatocytes;   

DOI  :  10.1016/0014-5793(82)80809-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Glucagon and insulin both stimulated the ³²P-labelling of ribosomal protein S6 in rat hepatocytes that had been incubated with ³²P_i. Glucagon selectively enhanced the labelling of the tryptic peptide phosphorylated by cyclic AMP-dependent protein kinase, demonstrating that 6 S is a physiological substrate for this enzyme. Insulin stimulated the phosphorylation of distinct tryptic peptides, at least one of which appears to be very close in the primary structure to the sites phosphorylated by cyclic AMP-dependent protein kinase.

【 授权许可】

Unknown