Heat shock increases the association of binding protein-1 with initiation factor 4E

Robert G.J. Vries, Andrea Flynn, Jashmin C. Patel, Xuemin Wang, Richard M. Denton, Christopher G. Proud

Research output: Contribution to journalArticlepeer-review

61 Citations (Scopus)

Abstract

The effects of heat shock on the regulation of the cap-binding initiation factor 4E (eIF4E) and its inhibitory binding protein, 4E-BP1, have been examined in Chinese hamster ovary cells and in cardiac myocytes. Heat shock increased the association between eIF4E and 4E-BP1, and this was associated with a dephosphorylation of 4E-BP1. These effects did not appear to be due wholly to decreased activity of the p70 S6 kinase pathways which is implicated in the control of 4E-BP1, and they were not mediated by the stress-activated p38 microtubule-associated protein kinase pathway. Increased binding of 4E-BP1 to eIF4E correlated with a decrease in the amount of eIF4G which co-purified with the latter. This could account for the previously observed impairment of eIF4F function during heat shock, and, since heat shock protein mRNAs are believed to be relatively cap-independent, could provide a mechanism for the selective up-regulation of the synthesis of heat shock proteins and other stress proteins during heat shock.

Original languageEnglish
Pages (from-to)32779-32784
Number of pages6
JournalJournal of Biological Chemistry
Volume272
Issue number52
DOIs
Publication statusPublished or Issued - 26 Dec 1997
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this