We are analyzing https://link.springer.com/article/10.1007/s10495-005-3088-0.

Title:
Role of the unfolded protein response in cell death | Apoptosis
Description:
Unfolded protein response (UPR) is an important genomic response to endoplasmic reticulum (ER) stress. The ER chaperones, GRP78 and Gadd153, play critical roles in cell survival or cell death as part of the UPR, which is regulated by three signaling pathways: PERK/ATF4, IRE1/XBP1 and ATF6. During the UPR, accumulated unfolded protein is either correctly refolded, or unsuccessfully refolded and degraded by the ubiquitin-proteasome pathway. When the unfolded protein exceeds a threshold, damaged cells are committed to cell death, which is mediated by ATF4 and ATF6, as well as activation of the JNK/AP-1/Gadd153-signaling pathway. Gadd153 suppresses activation of Bcl-2 and NF-κB. UPR-mediated cell survival or cell death is regulated by the balance of GRP78 and Gadd153 expression, which is coregulated by NF-κB in accordance with the magnitude of ER stress. Less susceptibility to cell death upon activation of the UPR may contribute to tumor progression and drug resistance of solid tumors.
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Keywords {🔍}

google, scholar, pubmed, cas, article, cell, protein, endoplasmic, reticulum, biol, response, stress, death, activation, apoptosis, unfolded, cancer, chem, factor, kim, caspase, atf, kinase, bcl, kaufman, cells, res, mol, biochem, grp, gadd, pathway, tumor, degradation, cytochrome, proteasome, research, role, signaling, expression, regulation, ire, wang, human, dev, genes, hiroshima, privacy, cookies, content,

Topics {✒️}

c-jun n-terminal kinase /camp-responsive-element-binding protein camp-response element-binding protein month download article/chapter er degradation-enhancing α-mannosidase hypoxia-inducible factor-1-dependent regulation jnk/ap-1/gadd153-signaling pathway apaf-1-independent intrinsic pathway ccaat/enhancer-binding protein time-dependent phase shift protein kinase/endoribonuclease ire1alpha mitochondria-dependent death cascades ros-mediated ask1 activation camp responsive element gadd153-mediated anticancer effects er-stress-mediated apoptosis acute proteasome-dependent degradation homologous protein/growth arrest mitochondrial apoptosis-inducing factor upr-mediated cell survival full article pdf endoplasmic reticulum ca2+ endoplasmic reticulum stress article apoptosis aims unfolded protein response unfolded-protein response pelizaeus-merzbacher disease akt/protein kinase privacy choices/manage cookies accumulated unfolded protein unfolded protein exceeds tumor necrosis factor jnk protein kinases activating transcription factor er chaperone grp78 gastric cancer cells mammalian ire1 autoregulates oakes sa gadd34-mediated dephosphorylation hypoxia-related therapies cellular redox state atp binding site proteasome inhibitor bortezomib cell death published programmed cell death protein accelerates er important genomic response blocking survival response free ca2+ concentration er alpha-mannosidase

Questions {❓}

Checkpoints in ER-associated degradation: Excuse me, which way to the proteasome?

Schema {🗺️}

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         headline:Role of the unfolded protein response in cell death
         description:Unfolded protein response (UPR) is an important genomic response to endoplasmic reticulum (ER) stress. The ER chaperones, GRP78 and Gadd153, play critical roles in cell survival or cell death as part of the UPR, which is regulated by three signaling pathways: PERK/ATF4, IRE1/XBP1 and ATF6. During the UPR, accumulated unfolded protein is either correctly refolded, or unsuccessfully refolded and degraded by the ubiquitin-proteasome pathway. When the unfolded protein exceeds a threshold, damaged cells are committed to cell death, which is mediated by ATF4 and ATF6, as well as activation of the JNK/AP-1/Gadd153-signaling pathway. Gadd153 suppresses activation of Bcl-2 and NF-κB. UPR-mediated cell survival or cell death is regulated by the balance of GRP78 and Gadd153 expression, which is coregulated by NF-κB in accordance with the magnitude of ER stress. Less susceptibility to cell death upon activation of the UPR may contribute to tumor progression and drug resistance of solid tumors.
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      headline:Role of the unfolded protein response in cell death
      description:Unfolded protein response (UPR) is an important genomic response to endoplasmic reticulum (ER) stress. The ER chaperones, GRP78 and Gadd153, play critical roles in cell survival or cell death as part of the UPR, which is regulated by three signaling pathways: PERK/ATF4, IRE1/XBP1 and ATF6. During the UPR, accumulated unfolded protein is either correctly refolded, or unsuccessfully refolded and degraded by the ubiquitin-proteasome pathway. When the unfolded protein exceeds a threshold, damaged cells are committed to cell death, which is mediated by ATF4 and ATF6, as well as activation of the JNK/AP-1/Gadd153-signaling pathway. Gadd153 suppresses activation of Bcl-2 and NF-κB. UPR-mediated cell survival or cell death is regulated by the balance of GRP78 and Gadd153 expression, which is coregulated by NF-κB in accordance with the magnitude of ER stress. Less susceptibility to cell death upon activation of the UPR may contribute to tumor progression and drug resistance of solid tumors.
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