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 journalArticle

33 Citations (Scopus)

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
Externally publishedYes

Fingerprint

Phosphorylation
Insulin Receptor
Serine
Protein Kinase C
Phosphotransferases
Peptides
Phosphoserine
Phosphopeptides
Electrophoresis, Gel, Two-Dimensional
Phorbol Esters
Cricetulus
Electrophoresis
Urea
Ovary
Gels
Chemical activation
Cells

Keywords

  • Insulin resistance
  • Protein kinase C
  • Tyrosine kinase

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Identification of serines-1035/1037 in the kinase domain of the insulin receptor as protein kinase Cα mediated phosphorylation sites. / Liu, Feng; Roth, Richard A.

In: FEBS Letters, Vol. 352, No. 3, 03.10.1994, p. 389-392.

Research output: Contribution to journalArticle

@article{027822fab6454023b84f992654ac2a4e,
title = "Identification of serines-1035/1037 in the kinase domain of the insulin receptor as protein kinase Cα mediated phosphorylation sites",
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.",
keywords = "Insulin resistance, Protein kinase C, Tyrosine kinase",
author = "Feng Liu and Roth, {Richard A.}",
year = "1994",
month = "10",
day = "3",
doi = "10.1016/0014-5793(94)00996-1",
language = "English (US)",
volume = "352",
pages = "389--392",
journal = "FEBS Letters",
issn = "0014-5793",
publisher = "Elsevier",
number = "3",

}

TY - JOUR

T1 - Identification of serines-1035/1037 in the kinase domain of the insulin receptor as protein kinase Cα mediated phosphorylation sites

AU - Liu, Feng

AU - Roth, Richard A.

PY - 1994/10/3

Y1 - 1994/10/3

N2 - 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.

AB - 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.

KW - Insulin resistance

KW - Protein kinase C

KW - Tyrosine kinase

UR - http://www.scopus.com/inward/record.url?scp=0028141653&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028141653&partnerID=8YFLogxK

U2 - 10.1016/0014-5793(94)00996-1

DO - 10.1016/0014-5793(94)00996-1

M3 - Article

C2 - 7926007

AN - SCOPUS:0028141653

VL - 352

SP - 389

EP - 392

JO - FEBS Letters

JF - FEBS Letters

SN - 0014-5793

IS - 3

ER -