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UPR IRE1

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https://www.readbyqxmd.com/read/29124827/recovery-from-temporary-er-stress-in-plants-relies-on-tissue-specific-and-largely-independent-roles-of-bzip28-and-bzip60-as-well-as-an-antagonizing-function-of-bax-inhibitor1-onto-the-pro-adaptive-signaling-mediated-by-bzip28
#1
Cristina Ruberti, YaShiuan Lai, Federica Brandizzi
The unfolded protein response (UPR) is an ancient signaling pathway that commits to life-or-death outcomes in response to proteotoxic stress in the endoplasmic reticulum (ER). In plants, the membrane-tethered transcription factor bZIP28 and the ribonuclease-kinase IRE1 along with its splicing target, bZIP60, govern the two cytoprotective UPR signaling pathways known to date. The conserved ER membrane-associated BAX inhibitor1 (BI1) modulates ER stress-induced programmed cell death through yet-unknown mechanisms...
November 10, 2017: Plant Journal: for Cell and Molecular Biology
https://www.readbyqxmd.com/read/29113324/unfolded-protein-response-signaling-impacts-macrophage-polarity-to-modulate-breast-cancer-cell-clearance-and-melanoma-immune-checkpoint-therapy-responsiveness
#2
David R Soto-Pantoja, Adam S Wilson, Kenysha Yj Clear, Brian Westwood, Pierre L Triozzi, Katherine L Cook
The unfolded protein response (UPR) is a stress pathway controlled by GRP78 to mediate IRE1, PERK, and ATF6 signaling. We show that targeting GRP78, IRE1, and PERK differentially regulates macrophage polarization. Specifically, PERK targeting enhanced macrophage proliferation and macrophage-mediated killing but not GRP78 or IRE1. Targeting UPR in cancer cells also differentially affected macrophage cytolytic capacity. Tumoral IRE1 or GRP78 inhibition enhanced macrophage-mediated cancer cell clearance. Conditioned media from GRP78-silenced cancer cells caused reciprocal regulation of CD80 and CD206, suggesting control of plasticity by secreted factors...
October 6, 2017: Oncotarget
https://www.readbyqxmd.com/read/29074489/autophagy-and-the-unfolded-protein-response-promote-pro-fibrotic-effects-of-tgf%C3%AE-1-in-human-lung-fibroblasts
#3
Saeid Ghavami, Behzad Yeganeh, Amir A Zeki, Shahla Shojaei, Nicholas J Kenyon, Sean Ott, Afshin Samali, John Patterson, Javad Alizadeh, Adel Rezaei Moghadam, Ian M C Dixon, Helmut Unruh, Darryl A Knight, Martin Post, Thomas Klonisch, Andrew John Halayko
BACKGROUND: Idiopathic pulmonary fibrosis (IPF) is a lethal fibrotic lung disease in adults with limited treatment options. Autophagy and the unfolded protein response (UPR), fundamental processes induced by cell stress, are dysregulated in lung fibroblasts and epithelial cells from humans with IPF. METHODS: Human primary cultured lung parenchymal and airway fibroblasts from non-IPF and IPF donors were stimulated with TGFβ1 with or without the inhibitors of autophagy or UPR (IRE1α inhibitor)...
October 26, 2017: American Journal of Physiology. Lung Cellular and Molecular Physiology
https://www.readbyqxmd.com/read/29044123/ire1%C3%AE-xbp1s-branch-of-upr-links-hif1%C3%AE-activation-to-mediate-angii-dependent-endothelial-dysfunction-under-particulate-matter-pm-2-5-exposure
#4
Xiuduan Xu, Aodeng Qimuge, Hongli Wang, Chen Xing, Ye Gu, Shasha Liu, Huan Xu, Meiru Hu, Lun Song
Short- and long-term exposure to particulate matter (PM) 2.5 instigates adverse health effect upon the cardiovascular (CV) system. Disclosing the molecular events by which PM2.5 evokes CV injuries is essential in developing effective risk-reduction strategy. Here we found that rats after intratracheally instillation with PM2.5 displayed increased circulating level of ANGII, the major bioactive peptide in renin-angiotensin-system (RAS), which resulted from the elevation of ANGII production in the vascular endothelium...
October 18, 2017: Scientific Reports
https://www.readbyqxmd.com/read/29024602/knockdown-of-cemip-suppresses-proliferation-and-induces-apoptosis-in-colorectal-cancer-cells-downregulation-of-grp78-and-attenuation-of-unfolded-protein-response
#5
Guodong Liang, Xuedong Fang, Yubo Yang, Yan Song
Cell migration inducing hyaluronan binding protein (CEMIP) has been suggested as a contributor in the carcinogenesis of colorectal cancer (CRC). Cancer cells can adapt to endoplasmic reticulum (ER) stress by initiating unfolded protein response (UPR). This study aimed at investigating whether CEMIP affected the UPR of CRC cells, with a focus on 78 kDa glucose-regulated protein (GRP78, a major ER chaperone). We found that knockdown of CEMIP inhibited cell proliferation and induced a G1 arrest in SW480 CRC cells...
October 12, 2017: Biochemistry and Cell Biology, Biochimie et Biologie Cellulaire
https://www.readbyqxmd.com/read/28971800/an-unfolded-protein-induced-conformational-switch-activates-mammalian-ire1
#6
Gülsün Elif Karagöz, Diego Acosta-Alvear, Hieu T Nguyen, Crystal P Lee, Feixia Chu, Peter Walter
The unfolded protein response (UPR) adjusts the cell's protein folding capacity in the endoplasmic reticulum (ER) according to need. IRE1 is the most conserved UPR sensor in eukaryotic cells. It has remained controversial, however, whether mammalian and yeast IRE1 use a common mechanism for ER stress sensing. Here, we show that similar to yeast, human IRE1α's ER-lumenal domain (hIRE1α LD) binds peptides with a characteristic amino acid bias. Peptides and unfolded proteins bind to hIRE1α LD's MHC-like groove and induce allosteric changes that lead to its oligomerization...
October 3, 2017: ELife
https://www.readbyqxmd.com/read/28952924/unfolded-protein-response-transducer-ire1-mediated-signaling-independent-of-xbp1-mrna-splicing-is-not-required-for-growth-and-development-of-medaka-fish
#7
Tokiro Ishikawa, Makoto Kashima, Atsushi J Nagano, Tomoko Ishikawa-Fujiwara, Yasuhiro Kamei, Takeshi Todo, Kazutoshi Mori
When activated by the accumulation of unfolded proteins in the endoplasmic reticulum, metazoan IRE1, the most evolutionarily conserved unfolded protein response (UPR) transducer, initiates unconventional splicing of XBP1 mRNA. Unspliced and spliced mRNA are translated to produce pXBP1(U) and pXBP1(S), respectively. pXBP1(S) functions as a potent transcription factor, whereas pXBP1(U) targets pXBP1(S) to degradation. In addition, activated IRE1 transmits two signaling outputs independent of XBP1, namely activation of the JNK pathway, which is initiated by binding of the adaptor TRAF2 to phosphorylated IRE1, and regulated IRE1-dependent decay (RIDD) of various mRNAs in a relatively nonspecific manner...
September 27, 2017: ELife
https://www.readbyqxmd.com/read/28945192/regulated-ire1-dependent-mrna-decay-requires-no-go-mrna-degradation-to-maintain-endoplasmic-reticulum-homeostasis-in-s-pombe
#8
Nicholas R Guydosh, Philipp Kimmig, Peter Walter, Rachel Green
The unfolded protein response (UPR) monitors and adjusts the protein folding capacity of the endoplasmic reticulum (ER). In S. pombe, the ER membrane-resident kinase/endoribonuclease Ire1 utilizes a mechanism of selective degradation of ER-bound mRNAs (RIDD) to maintain homeostasis. We used a genetic screen to identify factors critical to the Ire1-mediated UPR and found several proteins, Dom34, Hbs1 and Ski complex subunits, previously implicated in ribosome rescue and mRNA no-go-decay (NGD). Ribosome profiling in ER-stressed cells lacking these factors revealed that Ire1-mediated cleavage of ER-associated mRNAs results in ribosome stalling and mRNA degradation...
September 25, 2017: ELife
https://www.readbyqxmd.com/read/28929194/adapting-secretory-proteostasis-and-function-through-the-unfolded-protein-response
#9
Madeline Y Wong, Andrew S DiChiara, Patreece H Suen, Kenny Chen, Ngoc-Duc Doan, Matthew D Shoulders
Cells address challenges to protein folding in the secretory pathway by engaging endoplasmic reticulum (ER)-localized protective mechanisms that are collectively termed the unfolded protein response (UPR). By the action of the transmembrane signal transducers IRE1, PERK, and ATF6, the UPR induces networks of genes whose products alleviate the burden of protein misfolding. The UPR also plays instructive roles in cell differentiation and development, aids in the response to pathogens, and coordinates the output of professional secretory cells...
September 20, 2017: Current Topics in Microbiology and Immunology
https://www.readbyqxmd.com/read/28921568/neuronal-activity-dependent-local-activation-of-dendritic-unfolded-protein-response-promotes-expression-of-brain-derived-neurotrophic-factor-in-cell-soma
#10
Atsushi Saito, Longjie Cai, Koji Matsuhisa, Yosuke Ohtake, Masayuki Kaneko, Soshi Kanemoto, Rie Asada, Kazunori Imaizumi
Unfolded protein response (UPR) has roles not only in resolving the accumulation of unfolded proteins owing to endoplasmic reticulum (ER) stress, but also in regulation of cellular physiological functions. ER stress transducers providing the branches of UPR signaling are known to localize in distal dendritic ER of neurons. These reports suggest that local activation of UPR branches may produce integrated outputs for distant communication, and allow regulation of local events in highly polarized neurons. Here, we demonstrated that synaptic activity- and brain-derived neurotrophic factor (BDNF)-dependent local activation of UPR signaling could be associated with dendritic functions through retrograde signal propagation by using murine neuroblastoma cell line, Neuro-2A and primary cultured hippocampal neurons derived from postnatal day 0 litter C57BL/6 mice...
September 16, 2017: Journal of Neurochemistry
https://www.readbyqxmd.com/read/28915629/ier3ip1-deficiency-leads-to-increased-%C3%AE-cell-death-and-decreased-%C3%AE-cell-proliferation
#11
Juan Sun, Decheng Ren
Mutations in the gene for Immediate Early Response 3 Interacting Protein 1 (IER3IP1) cause permanent neonatal diabetes mellitus in human. The mechanisms involved have not been determined and the role of IER3IP1 in β-cell survival has not been characterized. In order to determine if there is a molecular link between IER3IP1 deficiency and β-cell survival and proliferation, we knocked down Ier3ip1 gene expression in mouse MIN6 insulinoma cells. IER3IP1 suppression induced apoptotic cell death which was associated with an increase in Bim and a decrease in Bcl-xL...
August 22, 2017: Oncotarget
https://www.readbyqxmd.com/read/28888981/hypoxia-in-3t3-l1-adipocytes-suppresses-adiponectin-expression-via-the-perk-and-ire1-unfolded-protein-response
#12
Qian Guo, Sanli Jin, Hailong Hu, Ying Zhou, Yuheng Yan, He Zong, Yu Wang, Hongjuan He, Yuri Oh, Chuanpeng Liu, Ning Gu
Adiponectin, an adipocytokine produced by adipocytes, functions as an anti-inflammatory and anti-apoptotic substance, while also enhancing insulin sensitivity. Patients or model animals with obesity or diabetes typically present attenuated expression of adiponectin. Moreover, obesity and diabetes are often accompanied with hypoxia in adipose tissue, which may result in endoplasmic reticulum (ER) stress as well as low expression of adiponectin. The purpose of this study was to investigate the specific role of the unfolded protein response (UPR) involved in the low expression of adiponectin induced by hypoxia...
November 4, 2017: Biochemical and Biophysical Research Communications
https://www.readbyqxmd.com/read/28886896/the-ire1-twist-that-links-proteostatic-with-lipostatic-control-of-the-endoplasmic-reticulum
#13
Tomás Aragón, Eelco van Anken
The unfolded protein response (UPR) governs homeostasis of both luminal content and membrane of the endoplasmic reticulum (ER). In Molecular Cell, Halbleib et al. identified how a twist in the juxta-membrane amphipathic helix of the UPR transducer Ire1 in yeast is essential for responding to both proteostatic and lipostatic ER stress.
October 2017: Trends in Cell Biology
https://www.readbyqxmd.com/read/28883998/endoplasmic-reticulum-stress-and-unfolded-protein-response-in-infection-by-intracellular-parasites
#14
REVIEW
Luca Galluzzi, Aurora Diotallevi, Mauro Magnani
Perturbations of the physiological status of the endoplasmic reticulum (ER) trigger a specific response known as the ER stress response or unfolded protein response (UPR). In mammalian cells, the UPR is mediated by three ER transmembrane proteins (IRE1, PERK and ATF6) which activate three signaling cascades to restore ER homeostasis. In recent years, a cross-talk between UPR, inflammatory and microbial sensing pathways has been elucidated. Pathogen infection can lead to UPR activation; moreover, several pathogens subvert the UPR to promote their survival and replication...
August 2017: Future Science OA
https://www.readbyqxmd.com/read/28882789/litopenaeus-vannamei-activating-transcription-factor-6-alpha-gene-involvement-in-er-stress-response-and-white-spot-symptom-virus-infection
#15
Kai Yuan, Hong-Hui He, Chao-Zheng Zhang, Xiao-Yun Li, Shao-Ping Weng, Jian-Guo He, Yi-Hong Chen
A previous study found that inositol-requiring enzyme-1-X-box binding protein 1 (IRE1-XBP1) pathway and the protein kinase RNA (PKR)-like ER kinase-eIF2α (PERK-eIF2α) pathway of shrimp play roles in the unfolded protein response (UPR). And they also be proved that was involved in white spot symptom virus (WSSV) infection. Yet the functions of the third branch in shrimp UPR are still unclear. In this study, we showed that upon UPR activation, activating transcription factor 6 alpha (LvATF6α) of Litopenaeus vannamei was cleaved and transferred from the cytoplasm to the nucleus in 293T cells, indicating that the ATF6 pathway in shrimp is also a branch of UPR...
September 4, 2017: Fish & Shellfish Immunology
https://www.readbyqxmd.com/read/28867719/er-stress-and-disease-toward-prevention-and-treatment
#16
Masayuki Kaneko, Kazunori Imaizumi, Atsushi Saito, Soshi Kanemoto, Rie Asada, Koji Matsuhisa, Yosuke Ohtake
Secretory and membrane proteins are synthesized in ribosomes, then mature in the endoplasmic reticulum (ER), but if ER function is impaired, immature defective proteins accumulate in the ER. This situation is called ER stress: in response, a defensive mechanism called the unfolded protein response (UPR) is activated in cells to reduce the defective proteins. During the UPR, the ER transmembrane sensor molecules inositol-requiring enzyme 1 (IRE1), activating transcription factor 6 (ATF6), and RNA-dependent protein kinase (PKR)-like ER kinase (PERK) are activated, stress signals are transduced to the outside of the ER, and various cell responses, including gene induction, occur...
2017: Biological & Pharmaceutical Bulletin
https://www.readbyqxmd.com/read/28832690/development-of-a-fluorescent-reporter-system-for-monitoring-er-stress-in-chinese-hamster-ovary-cells-and-its-application-for-therapeutic-protein-production
#17
Gargi Roy, Shu Zhang, Lina Li, Eileen Higham, Herren Wu, Marcello Marelli, Michael A Bowen
Mammalian cell expression systems have become a workhorse for the production of biotherapeutic proteins. As such, there is an ever increasing demand for higher productivity from these expression platforms to reduce manufacturing costs. While great advances have been made in the optimization of culture conditions and cell line selection to improve productivity, protein mis-folding remains a common limitation to high levels of production of therapeutic proteins. Accumulation of mis- and unfolded protein in the endoplasmic reticulum (ER) causes ER stress and initiates the unfolded protein response (UPR) that results in an activation of protein folding machinery, translation attenuation in an effort to proper folding of the newly synthesized peptides or may even lead to apoptosis if the correct folding is not restored...
2017: PloS One
https://www.readbyqxmd.com/read/28832521/opposite-roles-of-rnase-and-kinase-activities-of-inositol-requiring-enzyme-1-ire1-on-hsv-1-replication
#18
Airong Su, Huanru Wang, Yanlei Li, Xiaohui Wang, Deyan Chen, Zhiwei Wu
In response to the endoplasmic reticulum (ER) stress induced by herpes simplex virus type 1 (HSV-1) infection, host cells activate the unfolded protein response (UPR) to reduce the protein-folding burden in the ER. The regulation of UPR upon HSV-1 infection is complex, and the downstream effectors can be detrimental to viral replication. Therefore, HSV-1 copes with the UPR to create a beneficial environment for its replication. UPR has three branches, including protein kinase RNA (PKR)-like ER kinase (PERK), inositol-requiring enzyme 1 (IRE1), and activated transcription factor 6 (ATF6)...
August 23, 2017: Viruses
https://www.readbyqxmd.com/read/28794819/upregulation-of-autophagy-genes-and-the-unfolded-protein-response-in-human-heart-failure
#19
Brian C Jensen, Scott J Bultman, Darcy Holley, Wei Tang, Gustaaf de Ridder, Salvatore Pizzo, Dawn Bowles, Monte S Willis
The cellular environment of the mammalian heart constantly is challenged with environmental and intrinsic pathological insults, which affect the proper folding of proteins in heart failure. The effects of damaged or misfolded proteins on the cell can be profound and result in a process termed "proteotoxicity". While proteotoxicity is best known for its role in mediating the pathogenesis of neurodegenerative diseases such as Alzheimer's disease, its role in human heart failure also has been recognized. The UPR involves three branches, including PERK, ATF6, and IRE1...
2017: International Journal of Clinical and Experimental Medicine
https://www.readbyqxmd.com/read/28794014/iron-affects-ire1-clustering-propensity-and-the-amplitude-of-endoplasmic-reticulum-stress-signaling
#20
Nir Cohen, Michal Breker, Anush Bakunts, Kristina Pesek, Ainara Chas, Josepmaria Argemí, Andrea Orsi, Lihi Gal, Silvia Chuartzman, Yoav Wigelman, Felix Jonas, Peter Walter, Robert Ernst, Tomás Aragón, Eelco van Anken, Maya Schuldiner
The unfolded protein response (UPR) allows cells to adjust secretory pathway capacity according to need. Ire1, the endoplasmic reticulum (ER) stress sensor and central activator of the UPR is conserved from the budding yeast Saccharomyces cerevisiae to humans. Under ER stress conditions, Ire1 clusters into foci that enable optimal UPR activation. To discover factors that affect Ire1 clustering, we performed a high-content screen using a whole-genome yeast mutant library expressing Ire1-mCherry. We imaged the strains following UPR induction and found 154 strains that displayed alterations in Ire1 clustering...
October 1, 2017: Journal of Cell Science
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