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

RGJ Vries, A Flynn, JC Patel, XM Wang, RM Denton, CG Proud*

*Corresponding author for this work

Research output: Contribution to journalArticle (Academic Journal)peer-review

59 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-EP1, 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 pathway, 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
Publication statusPublished - 26 Dec 1997

Keywords

  • CAP-DEPENDENT TRANSLATION
  • EPIDIDYMAL FAT-CELLS
  • MESSENGER-RNA CAP
  • HELA-CELLS
  • PHAS-I
  • FACTOR EIF-4E
  • 3T3-L1 ADIPOCYTES
  • ALPHA-SUBUNIT
  • PHOSPHORYLATION
  • INSULIN

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