Results 81 to 90 of about 15,549 (206)
IRE1: ER stress sensor and cell fate executor [PDF]
Cells operate a signaling network termed the unfolded protein response (UPR) to monitor protein-folding capacity in the endoplasmic reticulum (ER). Inositol-requiring enzyme 1 (IRE1) is an ER transmembrane sensor that activates the UPR to maintain the ER and cellular function.
Yani, Chen, Federica, Brandizzi
openaire +2 more sources
Proteostasis ensures proper protein folding, modification, and degradation, while its impairment triggers ER stress. Chronic ER stress and maladaptive UPR via the CHOP–ERO1 axis remodel ERMCs, altering calcium signaling and mitochondrial metabolism.
Giorgia Maria Renna +5 more
wiley +1 more source
Expression of IGFBP6, IGFBP7, NOV, CYR61, WISP1 and WISP2 genes in U87 glioma cells in glutamine deprivation condition [PDF]
We have studied gene expression of insulin-like growth factor binding proteins in U87 glioma cells upon glutamine deprivation depending on the inhibition of IRE1 (inositol requiring enzyme-1), a central mediator of endoplasmic reticulum stress.
O. H. Minchenko +3 more
doaj +1 more source
Proteostasis of organelles in aging and disease
Cells rely on regulated proteostasis mechanisms to keep their internal compartments functioning properly. When these mechanisms fail, damaged proteins accumulate, disrupting organelles, such as the nucleus, mitochondria, endoplasmic reticulum, Golgi, and lysosomes, as well as membraneless organelles, such as stress granules, processing bodies, the ...
Yara Nabawi +5 more
wiley +1 more source
Interferon regulatory factor 4 mediates nonenzymatic IRE1 dependency in multiple myeloma cells.
Multiple myeloma (MM) arises through oncogenic transformation of immunoglobulin-secreting plasma cells. MM often co-opts the central endoplasmic reticulum (ER)-stress mitigator, inositol-requiring enzyme 1 (IRE1), to sustain malignant growth.
Ioanna Oikonomidi +9 more
doaj +1 more source
Proper protein folding in the endoplasmic reticulum (ER) is vital in all eukaryotes. When misfolded proteins accumulate in the ER lumen, the transmembrane kinase/endoribonuclease Ire1 initiates splicing of HAC1 mRNA to generate the bZIP transcription ...
Taiga Miyazaki +4 more
doaj +1 more source
Biogenesis of TNF‐α‐insights into proteostasis and inflammation
TNF‐α biogenesis, trafficking, and signalling are tightly and reciprocally coupled to cellular proteostasis systems, including ER chaperones and endoplasmic reticulum‐associated degradation. This bidirectional crosstalk determines whether TNF‐α responses are adaptive or proteotoxic.
Bailasan Haidar +3 more
wiley +1 more source
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.
Tokiro Ishikawa +6 more
doaj +1 more source
We investigated the potential of iloperidone as an activator of Sigma‐1 receptor (S1R) neuroprotective function in juvenile Huntington's disease (jHD). We tested iloperidone on cortical neurons differentiated from patient‐derived iPSCs, demonstrating that it acts as a S1R agonist, decreasing apoptosis, huntingtin aggregation, and oxidative stress ...
Ersilia Fornetti +11 more
wiley +1 more source
IRE1: a role in UPREgulation of ER degradation.
The unfolded protein response entered the mechanistic realm with the discovery of IRE1 as the key signal transducer in yeast. Although also found in mammals, it appeared to function in assisting the work of other players. The featured studies indicate a separate role for IRE1, and highlight the flexibility that bigger eukaryotes possess in this ...
openaire +2 more sources

