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

Feng Liu, Richard A. Roth

Research output: Contribution to journalArticlepeer-review

33 Scopus citations

Abstract

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.

Original languageEnglish (US)
Pages (from-to)389-392
Number of pages4
JournalFEBS Letters
Volume352
Issue number3
DOIs
StatePublished - Oct 3 1994

Keywords

  • Insulin resistance
  • Protein kinase C
  • Tyrosine kinase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Identification of serines-1035/1037 in the kinase domain of the insulin receptor as protein kinase Cα mediated phosphorylation sites'. Together they form a unique fingerprint.

Cite this