Corrigendum to ‘Oxidative stress-dependent activation of the eIF2α–ATF4 unfolded protein response branch by skin sensitizer 1-fluoro-2,4-dinitrobenzene modulates dendritic-like cell maturation and inflammatory status in a biphasic manner’

2015 ◽  
Vol 82 ◽  
pp. 203
Author(s):  
Andreia Luís ◽  
João Demétrio Martins ◽  
Ana Silva ◽  
Isabel Ferreira ◽  
Maria Teresa Cruz ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Unfolded Protein Response ◽  
Cell Maturation ◽  
Unfolded Protein ◽  
Inflammatory Status ◽  
Stress Dependent ◽  
Protein Response ◽  
Skin Sensitizer

Causal role of oxidative stress in unfolded protein response development in the hyperthyroid state

2015 ◽  
Vol 89 ◽  
pp. 401-408 ◽  
Author(s):  
Luis A. Videla ◽  
Virginia Fernández ◽  
Pamela Cornejo ◽  
Romina Vargas ◽  
Juan Carrasco ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Unfolded Protein Response ◽  
Causal Role ◽  
Unfolded Protein ◽  
Hyperthyroid State ◽  
Protein Response

scholarly journals HSP-4/BiP expression in secretory cells is regulated by a lineage-dependent differentiation program and not by the unfolded protein response

2018 ◽  
Author(s):  
Ji Zha ◽  
Jasmine Alexander-Floyd ◽  
Tali Gidalevitz
Keyword(s):  
Unfolded Protein Response ◽  
Secretory Cells ◽  
C Elegans ◽  
Unfolded Protein ◽  
Daughter Cells ◽  
Developmental Program ◽  
The Unfolded Protein Response ◽  
Stress Dependent ◽  
Protein Response ◽  
Anticipatory Activation

AbstractDifferentiation of secretory cells leads to sharp increases in protein synthesis, challenging ER proteostasis. Anticipatory activation of the unfolded protein response (UPR) prepares cells for the onset of secretory function by expanding the ER size and folding capacity. How cells ensure that the repertoire of induced chaperones matches their post-differentiation folding needs is not well understood. We find that during differentiation of stem-like seam cells, a typical UPR target, the C. elegans BiP homologue HSP-4, is selectively induced in alae-secreting daughter cells, but is repressed in hypodermal daughter cells. Surprisingly, this lineage-dependent induction bypasses the requirement for UPR signaling, and instead is controlled by a specific developmental program. The repression of HSP-4 in hypodermal-fated cells requires a transcriptional regulator BLMP-1/BLIMP1, involved in differentiation of mammalian secretory cells. The HSP-4 induction is anticipatory, and is required for the integrity of secreted alae. Thus, differentiation programs can directly control a broad-specificity chaperone that is normally stress-dependent, to ensure the integrity of secreted proteins.

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