Role of ERK1/ERK2 and p70S6K pathway in insulin signalling of protein synthesis

FEBS Lett. 1999 Mar 5;446(1):122-6. doi: 10.1016/s0014-5793(99)00193-3.

Abstract

The signalling pathways by which insulin triggers protein synthesis were studied using an antisense strategy to deplete ERK1/ERK2 and rapamycin to inhibit the p70S6K pathway. The results indicated that ERK1/ERK2 principally regulated the amount of the protein synthesis machinery available in the cell while the p70S6K pathway contributed to modulating its activation in response to insulin. ERK1/ERK2 also mediated in a small proportion of insulin-stimulated protein synthesis which included the induction of c-fos protein. When c-fos induction was blocked the majority of insulin-stimulated protein synthesis still occurred and thus did not require transcriptional regulation of c-fos or its targets.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adipocytes / metabolism*
  • Animals
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism*
  • Cell Line
  • Hypoglycemic Agents / metabolism
  • Hypoglycemic Agents / pharmacology*
  • Insulin / metabolism
  • Insulin / pharmacology*
  • Mice
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinases*
  • Protein Biosynthesis
  • Ribosomal Protein S6 Kinases / metabolism*
  • Signal Transduction / drug effects*

Substances

  • Hypoglycemic Agents
  • Insulin
  • Ribosomal Protein S6 Kinases
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Mitogen-Activated Protein Kinase 1
  • Mitogen-Activated Protein Kinase 3
  • Mitogen-Activated Protein Kinases