Identification of serines‐1035/1037 in the kinase domain of the insulin receptor as protein kinase Cα mediated phosphorylation sites

FEBS Letters

Roth, Richard A.¹  Liu, Feng¹ 

[1] Department of Molecular Pharmacology, Stanford University School of Medicine, Stanford, CA 94305, USA

关键词: Insulin resistance;    Tyrosine kinase;    Protein kinase C;   

DOI  :  10.1016/0014-5793(94)00996-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A new site of serine phosphorylation (Ser-1035/1037) has been identified in the kinase domain of the insulin receptor. Mutant receptors missing these two serines were expressed in Chinese hamster ovary cells overexpressing protein kinase Cα. These mutant receptors lacked a phorbol ester-stimulated phosphoserine containing tryptic peptide as demonstrated by both high percentage polyacrylamide/urea gel electrophoresis and two-dimensional tlc. Moreover, a synthetic peptide with the sequence of this tryptic peptide was phosphorylated by isolated protein kinase Cα, and co-migrated with the phosphopeptide from in vivo labeled receptor. These results indicate that serine-1035 and/or 1037 in the kinase domain of the insulin receptor are phosphorylated in response to activation of protein kinase Cα.

【 授权许可】

Unknown