Binding of SH2 containing proteins to the insulin receptor: A new way for modulating insulin signalling

Feng Liu, Richard A. Roth

Research output: Contribution to journalReview articlepeer-review

31 Scopus citations

Abstract

Prior studies have established a role in insulin action for the tyrosine phosphorylation of substrates and their subsequent complexing with SH2 containing proteins. More recently, SH2 proteins have been identified which can tightly bind to the tyrosine phosphorylated insulin receptor. The major protein identified so far (called Grb-IR or Grb10) of this type appears to be present in at least 3 isoforms, varying in the presence of a pleckstrin homology domain and in the sequence of its amino terminus. The binding of this protein to the insulin receptor appears to inhibit signalling by the receptor. The present review will discuss the current knowledge of the structure and function of this protein.

Original languageEnglish (US)
Pages (from-to)73-78
Number of pages6
JournalMolecular and Cellular Biochemistry
Volume182
Issue number1-2
DOIs
StatePublished - May 5 1998

Keywords

  • Insulin receptor
  • SH2 domains
  • Tyrosine phosphorylation

ASJC Scopus subject areas

  • Molecular Biology
  • Clinical Biochemistry
  • Cell Biology

Fingerprint Dive into the research topics of 'Binding of SH2 containing proteins to the insulin receptor: A new way for modulating insulin signalling'. Together they form a unique fingerprint.

Cite this