scholarly journals The effects of induced production of reactive oxygen species in organelles on endoplasmic reticulum stress and on the unfolded protein response in arabidopsis

2015 ◽  
Vol 116 (4) ◽  
pp. 541-553 ◽  
Author(s):  
Rengin Ozgur ◽  
Baris Uzilday ◽  
A. Hediye Sekmen ◽  
Ismail Turkan
Keyword(s):  
Reactive Oxygen Species ◽  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Unfolded Protein Response ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

scholarly journals Interplay between the unfolded protein response and reactive oxygen species: a dynamic duo

2018 ◽  
Vol 69 (14) ◽  
pp. 3333-3345 ◽  
Author(s):  
Rengin Ozgur ◽  
Baris Uzilday ◽  
Yuji Iwata ◽  
Nozomu Koizumi ◽  
Ismail Turkan
Keyword(s):  
Reactive Oxygen Species ◽  
Unfolded Protein Response ◽  
Reactive Oxygen ◽  
Oxygen Species ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

scholarly journals Human Cytomegalovirus Infection Activates and Regulates the Unfolded Protein Response

2005 ◽  
Vol 79 (11) ◽  
pp. 6890-6899 ◽  
Author(s):  
Jennifer A. Isler ◽  
Alison H. Skalet ◽  
James C. Alwine
Keyword(s):  
Endoplasmic Reticulum ◽  
Transcription Factor ◽  
Endoplasmic Reticulum Stress ◽  
Viral Infection ◽  
Unfolded Protein Response ◽  
Human Cytomegalovirus ◽  
Hcmv Infection ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

ABSTRACT Viral infection causes stress to the endoplasmic reticulum. The response to endoplasmic reticulum stress, known as the unfolded protein response (UPR), is designed to eliminate misfolded proteins and allow the cell to recover by attenuating translation and upregulating the expression of chaperones, degradation factors, and factors that regulate the cell's metabolic and redox environment. Some consequences of the UPR (e.g., expression of chaperones and regulation of the metabolism and redox environment) may be advantageous to the viral infection; however, translational attenuation would not. Thus, viruses may induce mechanisms which modulate the UPR, maintaining beneficial aspects and suppressing deleterious aspects. We demonstrate that human cytomegalovirus (HCMV) infection induces the UPR but specifically regulates the three branches of UPR signaling, PKR-like ER kinase (PERK), activating transcription factor 6 (ATF6), and inositol-requiring enzyme 1 (IRE-1), to favor viral replication. HCMV infection activated the eIF2α kinase PERK; however, the amount of phosphorylated eIF2α was limited and translation attenuation did not occur. Interestingly, translation of select mRNAs, which is dependent on eIF2α phosphorylation, did occur, including the transcription factor ATF4, which activates genes which may benefit the infection. The endoplasmic reticulum stress-induced activation of the transcription factor ATF6 was suppressed in HCMV-infected cells; however, specific chaperone genes, normally activated by ATF6, were activated by a virus-induced, ATF6-independent mechanism. Lastly, HCMV infection activated the IRE-1 pathway, as indicated by splicing of Xbp-1 mRNA. However, transcriptional activation of the XBP-1 target gene EDEM (ER degradation-enhancing α-mannosidase-like protein, a protein degradation factor) was inhibited. These results suggest that, although HCMV infection induces the unfolded protein response, it modifies the outcome to benefit viral replication.

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