Multisite serine phosphorylation of the insulin and IGF‐I receptors in transfected cells

FEBS Letters

Lammers, R.³  Siddle, K.¹  Pillay, T.S.¹  Whittaker, J.²  Ullrich, A.³ 

[1] Department of Clinical Biochemistry, University of Cambridge, Addenbrooke's Hospital, Hills Road, Cambridge, CB2 2QR, UK;Division of Endocrinology, Department of Medicine, Health Sciences Center, State University of New York, Stony Brook, NY 11794, USA;Department of Molecular Biology, Max-Planck-Institut für Biochemie, 8033 Martinsried bei München, Germany

关键词: Insulin;    IGF-I;    Protein kinase C;    Receptor;    Peptide mapping;    Phorbol ester;    PMA;    4β-phorbol 12β-myristate 13α-acetate;    SDS-PAGE;    Sodium Dodecyl sulphate-polyacrylamide gel electrophoresis;    DMSO;    Dimethylsulphoxide;    IGF-I;    insulin-like growth factor I;    PKC;    protein kinase C;   

DOI  :  10.1016/0014-5793(91)81035-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown