Identification of a phosphorylation site of the rat insulin receptor catalyzed by protein kinase C in an intact cell

FEBS Letters

Akanuma, Yasuo¹  Kasuga, Masato¹  Koshio, Osamu¹ 

[1] Institute for Diabetes Care and Research, Asahi Life Foundation, 1-6-1 Marunouchi, Chiyoda-ku, Tokyo 100, Japan

关键词: Insulin receptor;    Protein kinase C;    Phosphopeptide mapping;    two-dimensional;    Phosphothreonine;   

DOI  :  10.1016/0014-5793(89)81001-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In two-dimensional tryptic phosphopeptide mapping, the β-subunit of the insulin receptor phosphorylated by 12-O-tetra-decanoylphorbol-13-acetate in rat hepatoma cells (H-35) was separated into one phosphothreonine-containing peptide and several phosphoserine-containing peptides. The synthetic peptide coding residues 1327–1343 in the C-terminal region of the rat insulin receptor was phosphorylated at the threonine residue by protein kinase C in a phosphatidylserine and oleoylacetylglycerol dependent manner. Tryptic digest of this phosphopeptide migrated to the same position as the phosphothreonine containing peptide obtained from the β-subunit in two-dimensional phosphopeptide mapping. These data suggested that Thr 1336 of the insulin receptor is the site of phosphorylation by protein kinase C in intact cells.

【 授权许可】

Unknown