DDIT3 and KAT2A Proteins Regulate TNFRSF10A and TNFRSF10B Expression in Endoplasmic Reticulum Stress-mediated Apoptosis in Human Lung Cancer Cells

Li, Tianliang; Su, Ling; Lei, Yuanjiu; Liu, Xiangfang; Zhang, Yajing; Liu, Xiangguo

doi:10.1074/jbc.m115.645333

Cited by 100 publications

(98 citation statements)

References 49 publications

(69 reference statements)

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“…If the ER stress is resolved then the DR5 transcripts return to basal levels. Intriguingly, authors described that under persistent ER stress conditions DR5 accumulated in the ER or at the Golgi apparatus depending on the cell type, resulting on DR5 activation independently of TRAIL.Activation of the death receptor TRAIL-R1/DR4 has also been associated to ER stress [62]. It was shown that CHOP interacts with the phosphorylated form of the transcription factor JUN in a complex that binds to the AP-1 binding site within the DR4 promoter region.…”

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confidence: 99%

Cell death induced by endoplasmic reticulum stress

2015

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The endoplasmic reticulum (ER) is an organelle with multiple functions. The synthesis of transmembrane proteins and proteins that are to be secreted occur in this organelle. Many Author ManuscriptThis article is protected by copyright. All rights reserved conditions that impose stress to the cells, including hypoxia, starvation, infections and changes in secretory needs challenge the folding capacity of the cell and promote ER stress. The cellular response involves the activation of sensors that transduce signaling cascades with the aim to restore homeostasis. This is known as the Unfolded Protein Response (UPR), which also intersects with the Integrated Stress Response (ISR) that reduces protein synthesis through inactivation of the initiation factor eIF2α. Central to the UPR are the sensors PERK, IRE1 and ATF6, as well as other signaling nodes such as JNK and the downstream transcription factors XBP-1, ATF4 and CHOP. These proteins aim to restore homeostasis but they can also induce cell death, which has been shown to occur by necroptosis and, more commonly, through the regulation of Bcl-2 family proteins (Bim, Noxa and Puma) that leads to mitochondrial apoptosis. Additionally, ER stress and proteotoxic stress have been shown to induce TRAIL receptors and activation of Caspase-8.ER stress is a common feature in the pathology of numerous diseases as it plays a role in neurodegeneration, stroke, cancer, metabolic diseases and inflammation. Understanding how cells react to ER stress can accelerate discovery of drugs against these diseases. KeywordsEndoplasmic reticulum stress The endoplasmic reticulum and the Unfolded Protein Response sensorsThe endoplasmic reticulum (ER) is the organelle where transmembrane proteins and proteins that are going to be secreted are synthesized and folded. This organelle, however, is essential for multiple other cellular functions such as Ca 2+ buffering, biosynthesis of phospholipids and cholesterol. Synthesis of proteins, cholesterol and some metabolites is an ATP demanding process that also requires the right ionic strength. Disturbances in many homeostatic processes will thus lead to a state in which protein folding slows down (ER stress). The subsequent accumulation of misfolded or unfolded proteins will indicate problems in cellular homeostasis that frequently end up in cell death.Problems in protein folding can occur due to stressors apparently disparate such as starvation or viral infection. These stimuli promote the activation of a series of signals that promote synthesis of new proteins to cope with stress while reducing general protein synthesis [1,2]. This is called the Unfolded Protein Response (UPR). Another way by which the UPR aims to restore homeostasis is the stimulation of protein degradation via autophagy and the enhanced clearance of unfolded proteins by a process termed ER-Associated Degradation (ERAD).The UPR is orchestrated by three main sensors that reside in the membrane of the ER. These transmembrane proteins bind to the chaperone GRP78/BiP in the...

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Cell death induced by endoplasmic reticulum stress

2015

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“…A B С tion IRE1 signaling causes down-regulation of this gene expression, because it was recently shown that DDIT3 and KAT2A proteins regulate TNFRSF10B expression in endoplasmic reticulum stress-mediated apoptosis in human lung cancer cells [20]. However, glucose deprivation has an opposite effect on this gene expression.…”

Section: Fig 3 Effect Of Glucose Deprivation Condition On the Exprementioning

confidence: 99%

“…Conversely the decoy receptors TRAILR3 and TRAILR4, which lack the pro-apoptotic death domain, function to dampen the apoptotic response by competing for TRAIL ligand. TRAILR4 does not induce apoptosis, and has been shown to play an inhibitory role in TRAIL-induced cell apoptosis [20,21,24].…”

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“…Moreover, pancreatic tumor samples have increased levels of nuclear TRAILR2, which correlate with poor outcome of patients. Recently, it was shown that TNFRSF10B expression was essential for endoplasmic reticulum stress-mediated apoptosis in human lung cancer cells [20]. TNF receptor signaling is controlled by a set of adaptor molecules and has significant potential to exert pro-survival and protective roles in several diseases [31].…”

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“…However, the executive mechanisms of the exhibited anti-proliferative effects are not yet known. It is possible that anti-proliferative effect is also realized through mediation by tumor necrosis factor (TNF) and its receptors signaling, which are integrated into the UPR signaling pathways, to regulate cell apoptosis and proliferation [19][20][21][22][23]. Possible involvement of tumor necrosis factor receptor superfamily (TNFRSF) proteins such as TNFRSF21/DR6, TNFRSF10B/DR5/TRAILR2, TNFRSF10D/TRAILR4, TNFRSF11B, and TNFRS-F1A as well as TNFα-induced proteins was made evi dently pertinent through transcriptomic analysis of U87 glioma cells expressing the dominant-negative mutant of IRE1 [18].…”

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Inhibition of IRE1 modifies effect of glucose deprivation on the expression of TNF?-related genes in U87 glioma cells

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et al. 2015

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Pirin Inhibits FAS‐Mediated Apoptosis to Support Colorectal Cancer Survival

Ma,

Suleman,

Zhang

et al. 2023

Advanced Science

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Resistance to immunotherapy in colorectal cancer (CRC) is associated with obstruction of FAS (Apo‐1 or CD95)‐dependent apoptosis, a hallmark of cancer. Here it is demonstrated that the upregulation of pirin (PIR) protein in colon cancers promotes tumorigenesis. Knockout or inhibition of PIR dramatically increases FAS expression, FAS‐dependent apoptosis and attenuates colorectal tumor formation in mice. Specifically, NFκB2 is a direct transcriptional activator of FAS and robustly suppressed by PIR in dual mechanisms. One is the disruption of NFκB2 complex (p52‐RELB) association with FAS promoter, the other is the inhibition of NIK‐mediated NFκB2 activation and nuclear translocation, leading to the inability of active NFκB2 complex toward the transcription of FAS. Furthermore, PIR interacts with FAS and recruits it in cytosol, preventing its membrane translocation and assembling. Importantly, knockdown or knockout of PIR dramatically sensitizes cells to FAS mAb‐ or active CD8+ T cells‐triggered cell death. Taken together, a PIR‐NIK‐NFκB2‐FAS survival pathway is established, which plays a key role in supporting CRC survival.

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DDIT3 and KAT2A Proteins Regulate TNFRSF10A and TNFRSF10B Expression in Endoplasmic Reticulum Stress-mediated Apoptosis in Human Lung Cancer Cells

Cited by 100 publications

References 49 publications

Cell death induced by endoplasmic reticulum stress

Cell death induced by endoplasmic reticulum stress

Inhibition of IRE1 modifies effect of glucose deprivation on the expression of TNF?-related genes in U87 glioma cells

Pirin Inhibits FAS‐Mediated Apoptosis to Support Colorectal Cancer Survival

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