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Review
, 110 (10), 1383-8

Translational Control in the Endoplasmic Reticulum Stress Response

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Review

Translational Control in the Endoplasmic Reticulum Stress Response

David Ron. J Clin Invest.

Figures

Figure 1
Figure 1
The functional components of the mammalian ER stress response. An imbalance between load of client proteins imposed on the ER and its capacity to fold them triggers a tripartite stress response. Genes whose products increase the functional capacity of the ER or enhance ER-associated protein degradation are activated. Translation is inhibited, and the flux of client proteins is thereby attenuated. Cell death pathways are activated. The first two components of the response enhance the resistance of cells to ER stress, whereas the last component is presumably adaptive at the organism level.
Figure 2
Figure 2
Signaling in the integrated stress response (ISR). ER stress, nutrient deprivation, oxidative stress, and hibernation are all associated with elevated eIF2α phosphorylation. The first two activate known eIF2α kinases, whereas the others act through unknown mechanisms. Phosphorylation of this factor inhibits translation of most mRNAs, leading to a decline in protein synthesis rates. Paradoxically, the translation of the transcription factor ATF4 is increased, increasing the transcription of specific target genes under conditions of ER stress. Expression of one of these target genes, GADD34, may set the stage for the resumption of mRNA translation after ER stress is resolved.

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