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

Vries, Robert G., Flynn, Andrea, Patel, Jashmin, Wang, Xuemin, Denton, Richard M., 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. (doi:10.1074/jbc.272.52.32779) (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)

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. (Contact us about this Publication)
Official URL
http://dx.doi.org/10.1074/jbc.272.52.32779

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.

Item Type: Article
DOI/Identification number: 10.1074/jbc.272.52.32779
Subjects: Q Science > QP Physiology (Living systems)
Divisions: Faculties > Sciences > School of Biosciences
Depositing User: T.J. Sango
Date Deposited: 07 Mar 1914 04:20 UTC
Last Modified: 28 May 2019 13:56 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/18013 (The current URI for this page, for reference purposes)
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