TY - JOUR
T1 - Heat shock increases the association of binding protein-1 with initiation factor 4E
AU - Vries, Robert G.J.
AU - Flynn, Andrea
AU - Patel, Jashmin C.
AU - Wang, Xuemin
AU - Denton, Richard M.
AU - Proud, Christopher G.
N1 - Copyright:
Copyright 2007 Elsevier B.V., All rights reserved.
PY - 1997/12/26
Y1 - 1997/12/26
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0031439105&partnerID=8YFLogxK
U2 - 10.1074/jbc.272.52.32779
DO - 10.1074/jbc.272.52.32779
M3 - Article
C2 - 9407052
AN - SCOPUS:0031439105
SN - 0021-9258
VL - 272
SP - 32779
EP - 32784
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 52
ER -