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

Authors :
Vries RG
Flynn A
Patel JC
Wang X
Denton RM
Proud CG
Source :
The Journal of biological chemistry [J Biol Chem] 1997 Dec 26; Vol. 272 (52), pp. 32779-84.
Publication Year :
1997

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 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.

Details

Language :
English
ISSN :
0021-9258
Volume :
272
Issue :
52
Database :
MEDLINE
Journal :
The Journal of biological chemistry
Publication Type :
Academic Journal
Accession number :
9407052
Full Text :
https://doi.org/10.1074/jbc.272.52.32779