Getting RIDD of RNA: IRE1 in cell fate regulation

Maurel, M.; Chevet, Éric; Tavernier, Jan; Gerlo, Sarah

doi:10.1016/j.tibs.2014.02.008

Cited by 514 publications

(465 citation statements)

References 80 publications

Supporting

Mentioning

454

Contrasting

Order By: Relevance

“…18 In addition, ANG cleaves the conserved singlestranded 39-CCA termini of all tRNAs, thereby promoting the deactivation of the aminoacyl-ends of tRNA and subsequently inhibiting translation. 43 Therefore, ANG participates in translation attenuation in ER-stressed cells through an original process of RNA interference which therefore expands UPR-induced mechanisms for the reduction of protein flux into the ER and comes in addition to the previously described phosphorylation of eIF2a, 44 regulated IRE1a-dependent decay of RNAs, 36 and selective mRNA release from the ER. 45 Our data also indicate that in the first hours after ER stress induction, ANG-mediated translation repression correlates with ANG dissociation from the ANG-inhibitor RNH1.…”

Section: Discussionmentioning

confidence: 96%

“…Notably, the activity of ANG on protein translation and SG formation was likely independent of eIF2a phosphorylation, as previously described during oxidative stress, 15 because the inhibition of ANG expression did not alter ER stress-induced eIF2a phosphorylation ( Figure 4F). The inhibition of ANG expression was not associated with degradation of total RNA, which could impact protein synthesis rate 35,36 ( Figure 4G). In addition, ANG silencing was associated with the increased production of the spliced product of X-box binding protein 1 (XBP1) mRNA, sXBP1, likely reflecting the exacerbation of misfolding burden on ER due to deficient inhibition of protein synthesis ( Figure 4H).…”

Section: Ang Participates In Translation Inhibition During Er Stressmentioning

confidence: 99%

See 1 more Smart Citation

Angiogenin Mediates Cell-Autonomous Translational Control under Endoplasmic Reticulum Stress and Attenuates Kidney Injury

Mami

Bouvier

Karoui

et al. 2016

Journal of the American Society of Nephrology

View full text Add to dashboard Cite

Endoplasmic reticulum (ER) stress is involved in the pathophysiology of kidney disease and aging, but the molecular bases underlying the biologic outcomes on the evolution of renal disease remain mostly unknown. Angiogenin (ANG) is a ribonuclease that promotes cellular adaptation under stress but its contribution to ER stress signaling remains elusive. In this study, we investigated the ANG-mediated contribution to the signaling and biologic outcomes of ER stress in kidney injury. ANG expression was significantly higher in samples from injured human kidneys than in samples from normal human kidneys, and in mouse and rat kidneys, ANG expression was specifically induced under ER stress. In human renal epithelial cells, ER stress induced ANG expression in a manner dependent on the activity of transcription factor XBP1, and ANG promoted cellular adaptation to ER stress through induction of stress granules and inhibition of translation. Moreover, the severity of renal lesions induced by ER stress was dramatically greater in ANG knockout mice (Ang 2/2 ) mice than in wild-type mice. These results indicate that ANG is a critical mediator of tissue adaptation to kidney injury and reveal a physiologically relevant ER stressmediated adaptive translational control mechanism.

show abstract

Section: Discussionmentioning

confidence: 96%

Section: Ang Participates In Translation Inhibition During Er Stressmentioning

confidence: 99%

Angiogenin Mediates Cell-Autonomous Translational Control under Endoplasmic Reticulum Stress and Attenuates Kidney Injury

Mami

Bouvier

Karoui

et al. 2016

Journal of the American Society of Nephrology

View full text Add to dashboard Cite

show abstract

“…Regulated IRE1-dependent decay of mRNA, a key component of the unfolded protein response, results in degradation of viral mRNA transcripts and spliced Xbp1 (13,35). However, there are multiple lines of evidence suggesting that IRF3 activation can result from other forms of noninfectious cell damage that involve Xbp1 splicing (17,18,36).…”

Section: Discussionmentioning

confidence: 99%

“…Excessive ER stress is associated with pro-apoptotic signaling and can be pathogenic (13,14). To test whether CCl 4 -induced acute hepatocyte injury induces an early ER stress response, we analyzed livers of mice at various time points after a single administration of CCl 4 .…”

Section: Irf3 Deficiency Attenuates Chronic CCL 4 -Mediated Livermentioning

confidence: 99%

Endoplasmic Reticulum Stress-induced Hepatocellular Death Pathways Mediate Liver Injury and Fibrosis via Stimulator of Interferon Genes

Iracheta-Vellve

Petrášek

Gyöngyösi

et al. 2016

Journal of Biological Chemistry

128

119

View full text Add to dashboard Cite

Edited by Jeffrey PessinFibrosis, driven by inflammation, marks the transition from benign to progressive stages of chronic liver diseases. Although inflammation promotes fibrogenesis, it is not known whether other events, such as hepatocyte death, are required for the development of fibrosis. Interferon regulatory factor 3 (IRF3) regulates hepatocyte apoptosis and production of type I IFNs. In the liver, IRF3 is activated via Toll-like receptor 4 (TLR4) signaling or the endoplasmic reticulum (ER) adapter, stimulator of interferon genes (STING). We hypothesized that IRF3-mediated hepatocyte death is an independent determinant of chemically induced liver fibrogenesis. To test this, we performed acute or chronic CCl 4 administration to WT and IRF3-, Toll/ Interleukin-1R (TIR) domain-containing adapter-inducing interferon-␤ (TRIF)-, TRIF-related adaptor molecule (TRAM)-, and STING-deficient mice. We report that acute CCl 4 administration to WT mice resulted in early ER stress, activation of IRF3, and type I IFNs, followed by hepatocyte apoptosis and liver injury, accompanied by liver fibrosis upon repeated administration of CCl 4 . Deficiency of IRF3 or STING prevented hepatocyte death and fibrosis both in acute or chronic CCl 4 . In contrast, mice deficient in type I IFN receptors or in TLR4 signaling adaptors, TRAM or TRIF, upstream of IRF3, were not protected from hepatocyte death and/or fibrosis, suggesting that the proapoptotic role of IRF3 is independent of TLR signaling in fibrosis. Hepatocyte death is required for liver fibrosis with causal involvement of STING and IRF3. Thus, our results identify that IRF3, by its association with STING in the presence of ER stress, couples hepatocyte apoptosis with liver fibrosis and indicate that innate immune signaling regulates outcomes of liver fibrosis via modulation of hepatocyte death in the liver.

show abstract

“…Th is stress is recognized as an important determinant of cancer and contributes to the expression profi le of many regulatory genes resulting in proliferation, apoptosis, angiogenesis, and circadian clock (Clarke et al 2014;Manie et al 2014;Pluquet et al 2014;Dejeans et al 2015;Minchenko et al 2015). Th e IRE1 enzyme is responsible for degradation of a specifi c subset of mRNA and alternative splicing of the XBP1 (X-box binding protein 1) transcription factor mRNA for control of the expression of unfolded protein response-specifi c genes (Acosta-Alvear et al 2007;Aragon et al 2009;Dejeans et al 2012;Pluquet et al 2013;Maurel et al 2014Maurel et al , 2015.…”

mentioning

confidence: 99%

Hypoxic regulation of the expression of genes encoded estrogen related proteins in U87 glioma cells: eff ect of IRE1 inhibition

et al. 2017

Endocrine Regulations

View full text Add to dashboard Cite

Objective. Th e aim of the present study was to examine the eff ect of inhibition of endoplasmic reticulum stress signaling, mediated by IRE1 (inositol requiring enzyme 1), which is a central mediator of the unfolded protein response on the expression of genes encoded estrogen related proteins (NRIP1/RIP140, TRIM16/EBBP, ESRRA/NR3B1, FAM162A/E2IG5, PGRMC2/PMBP, and SLC39A6/LIV-1) and their hypoxic regulation in U87 glioma cells for evaluation of their possible signifi cance in the control of glioma cells proliferation.Methods. Th e expression of NRIP1, EBBP, ESRRA, E2IG5, PGRMC2, and SLC39A6 genes in U87 glioma cells, transfected by empty vector pcDNA3.1 (control) and cells without IRE1 signaling enzyme function (transfected by dnIRE1) upon hypoxia, was studied by a quantitative polymerase chain reaction.Results. Inhibition of both enzymatic activities (kinase and endoribonuclease) of IRE1 signaling enzyme function up-regulates the expression of EBBP, E2IG5, PGRMC2, and SLC39A6 genes is in U87 glioma cells in comparison with the control glioma cells, with more signifi cant changes for E2IG5 and PGRMC2 genes. At the same time, the expression of NRIP1 and ESRRA genes is strongly down-regulated in glioma cells upon inhibition of IRE1. We also showed that hypoxia increases the expression of E2IG5, PGRMC2, and EBBP genes and decreases NRIP1 and ESRRA genes expression in control glioma cells. Furthermore, the inhibition of IRE1 in U87 glioma cells decreases the eff ect of hypoxia on the expression of E2IG5 and PGRMC2 genes, eliminates hypoxic regulation of NRIP1 gene, and enhances the sensitivity of ESRRA gene to hypoxic condition. Furthermore, the expression of SLC39A6 gene is resistant to hypoxia in both the glioma cells with and without IRE1 signaling enzyme function. Conclusions.Results of this investigation demonstrate that inhibition of IRE1 signaling enzyme function aff ects the expression of NRIP1, EBBP, ESRRA, E2IG5, PGRMC2, and SLC39A6 genes in U87 glioma cells in gene specifi c manner and these changes possibly contribute to the suppression of the cell proliferation. Most of these genes are regulated by hypoxia and preferentially through IRE1 signaling pathway of endoplasmic reticulum stress.

show abstract

Getting RIDD of RNA: IRE1 in cell fate regulation

Cited by 514 publications

References 80 publications

Angiogenin Mediates Cell-Autonomous Translational Control under Endoplasmic Reticulum Stress and Attenuates Kidney Injury

Angiogenin Mediates Cell-Autonomous Translational Control under Endoplasmic Reticulum Stress and Attenuates Kidney Injury

Endoplasmic Reticulum Stress-induced Hepatocellular Death Pathways Mediate Liver Injury and Fibrosis via Stimulator of Interferon Genes

Hypoxic regulation of the expression of genes encoded estrogen related proteins in U87 glioma cells: eff ect of IRE1 inhibition

Contact Info

Product

Resources

About