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

Vries, Robert G. and Flynn, Andrea and Patel, Jashmin and Wang, Xuemin and Denton, Richard M. and Proud, Christopher G. (1997) Heat shock increases the association of binding protein-1 with initiation factor 4E. Journal of Biological Chemistry, 272 (52). pp. 32779-32784. ISSN 0021-9258. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided)

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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.

Item Type: Article
Subjects: Q Science > QP Physiology (Living systems)
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: T.J. Sango
Date Deposited: 07 Mar 1914 04:20
Last Modified: 11 Jun 2014 08:37
Resource URI: https://kar.kent.ac.uk/id/eprint/18013 (The current URI for this page, for reference purposes)
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