Insulin stimulates protein synthesis in skeletal muscle by enhancing the association of eIF-4E and eIF-4G

Scot R. Kimball, Christine V. Jurasinski, John C. Lawrence, Leonard S. Jefferson

Research output: Contribution to journalArticle

155 Scopus citations

Abstract

Insulin stimulated protein synthesis in gastrocnemius muscle of perifused rat hindlimb preparations by approximately twofold. The stimulation of protein synthesis was associated with a 12-fold increase in the amount of eukaryotic initiation factor eIF-4G bound to the mRNA cap-binding protein eIF-4E. In part, the increased binding of eIF-4G to eIF-4E was a result of release of eIF-4E bound to the translational regulator, PHAS-I, through a mechanism involving enhanced phosphorylation of PHAS-I. However, the insulin- induced association of eIF-4E and eIF-4G was not due to increased net phosphorylation of eIF-4E because insulin decreased the amount present in the phosphorylated form from 86 to 59% of total eIF-4E. Overall, the results suggest that insulin stimulates protein synthesis in gastrocnemius muscle through a mechanism involving increased binding of eIF-4G to eIF-4E, which is in part due to phosphorylation of PHAS-I, resulting in a release of eIF-4E from the inactive PHAS-I. eIF-4E complex.

Original languageEnglish (US)
Pages (from-to)C754-C759
JournalAmerican Journal of Physiology - Cell Physiology
Volume272
Issue number2 41-2
DOIs
StatePublished - Feb 1997

All Science Journal Classification (ASJC) codes

  • Physiology
  • Cell Biology

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