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Multisite serine phosphorylation of the insulin and IGF‐I receptors in transfected cells
Author(s) -
Pillay T.S.,
Whittaker J.,
Lammers R.,
Ullrich A.,
Siddle K.
Publication year - 1991
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(91)81035-7
Subject(s) - phosphoserine , phosphorylation , serine , receptor , chemistry , insulin receptor , transfection , biochemistry , peptide , insulin , biology , endocrinology , insulin resistance , gene
Serine phosphorylation of insulin/IGF‐I receptors in transfected fibroblasts was analysed by peptide mapping, PMA stimulated the phosphorylation of 5 distinct insulin receptor phosphopeptides: a single major phosphothreonine peptide containing Thr‐1348, one major and 3 minor phosphoserine peptides. The major insulin‐stimulated phosphoserine peptides were the same as those after PMA, with the exception of 2 minor phosphoserine peptides. PMA stimulated phosphorylation of a single major IGF‐I receptor phosphoserine peptide which was phosphorylated to a lesser extent after IGF‐I. We conclude that insulin/IGF‐I and PMA stimulate phosphorylation of the same sites, but differ in the extents of phosphorylation.