The IRS-signalling system: a network of docking proteins that mediate insulin action

Mol Cell Biochem. 1998 May;182(1-2):3-11.

Abstract

New molecules discovered during the past ten years have created a rational framework to understand signalling transduction by a broad range of growth factors and cytokines, including insulin. Insulin action is initiated through the insulin receptor, a transmembrane glycoprotein with intrinsic protein tyrosine kinase activity. The tyrosine kinase mediates the insulin response through tyrosine phosphorylation of various cellular substrates, in particular the IRS-proteins. During insulin-stimulated tyrosine phosphorylation, the IRS-proteins mediate a broad biological response by binding and activating various enzymes or adapter molecules. Although we are far from a complete understanding of the insulin signalling system and its failure, enough pieces of the puzzle are falling into place that mechanism-based solutions to insulin resistance encountered with type II diabetes may soon be attainable.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Adaptor Proteins, Signal Transducing
  • Animals
  • DNA-Binding Proteins*
  • Humans
  • Insulin / physiology*
  • Insulin Receptor Substrate Proteins
  • Intracellular Signaling Peptides and Proteins
  • Phosphoproteins / physiology*
  • RNA-Binding Proteins*
  • Receptor, Insulin / physiology*
  • Signal Transduction*

Substances

  • Adaptor Proteins, Signal Transducing
  • DNA-Binding Proteins
  • DOK1 protein, human
  • Dok1 protein, mouse
  • GAB1 protein, human
  • GAP-associated protein p62
  • Gab1 protein, mouse
  • IRS1 protein, human
  • IRS2 protein, human
  • IRS3P protein, human
  • Insulin
  • Insulin Receptor Substrate Proteins
  • Intracellular Signaling Peptides and Proteins
  • Irs1 protein, mouse
  • Irs2 protein, mouse
  • Phosphoproteins
  • RNA-Binding Proteins
  • Receptor, Insulin