tailieunhanh - Báo cáo Y học: Cellular stresses profoundly inhibit protein synthesis and modulate the states of phosphorylation of multiple translation factors

We have examined the effects of widely used stress-inducing agents on protein synthesis and on regulatory components of the translational machinery. The three stresses chosen, arsenite, hydrogen peroxide and sorbitol, exert their effects in quite different ways. Nonetheless, all three rapidly ( 30 min) caused a profound inhibition of protein synthesis. In each case this was accompanied by dephosphorylation of the eukaryotic initiation factor (eIF) 4E-binding protein 1 (4E-BP1) and increased binding of this repressor protein to eIF4E. . | Eur. J. Biochem. 269 3076-3085 2002 FEBS 2002 doi Cellular stresses profoundly inhibit protein synthesis and modulate the states of phosphorylation of multiple translation factors Jashmin Patel1 Laura E. McLeod2 Robert G. J. Vries1 Andrea Flynn1 Xuemin Wang1 2 and Christopher G. Proud1 2 1Department of Biosciences University of Kent at Canterbury Canterbury UK 2Division of Molecular Physiology School of Life Sciences University of Dundee UK We have examined the effects of widely used stress-inducing agents on protein synthesis and on regulatory components of the translational machinery. The three stresses chosen arsenite hydrogen peroxide and sorbitol exert their effects in quite different ways. Nonetheless all three rapidly w 30 min caused a profound inhibition of protein synthesis. In each case this was accompanied by dephosphorylation of the eukaryotic initiation factor eIF 4E-binding protein 1 4E-BP1 and increased binding of this repressor protein to eIF4E. Binding of 4E-BP1 to eIF4E correlated with loss of eIF4F complexes. Sorbitol and hydrogen peroxide each caused inhibition of the 70-kDa ribosomal protein S6 kinase while arsenite activated it. The effects of stresses on the phosphorylation of eukaryotic elongation factor 2 also differed oxidative stress elicited a marked increase in eEF2 phosphorylation which is expected to contribute to inhibition of translation while the other stresses did not have this effect. Although all three proteins 4E-BP1 p70 S6 kinase and eEF2 can be regulated through the mammalian target of rapamycin mTOR our data imply that stresses do not interfere with mTOR function but act in different ways on these three proteins. All three stresses activate the p38 MAP kinase pathway but we were able to exclude a role for this in their effects on 4E-BP1. Our data reveal that these stress-inducing agents which are widely used to study stress-signalling in mammalian cells exert multiple and complex inhibitory .

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