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Identification of a phosphorylation site of the rat insulin receptor catalyzed by protein kinase C in an intact cell
Author(s) -
Koshio Osamu,
Akanuma Yasuo,
Kasuga Masato
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81001-4
Subject(s) - phosphopeptide , phosphoserine , biochemistry , phosphorylation , threonine , protein subunit , chemistry , protein kinase a , insulin receptor , peptide , protein kinase c , microbiology and biotechnology , biology , insulin , serine , insulin resistance , endocrinology , gene
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.