Results 71 to 80 of about 15,094 (184)
IRE1 RNase controls CD95-mediated cell death
Abstract Signalling by the Unfolded Protein Response (UPR) or by the Death Receptors (DR) are frequently activated towards pro-tumoral outputs in cancer. Herein, we demonstrate that the UPR sensor IRE1 controls the expression of the DR CD95/Fas, and its cell death-inducing ability.
Pelizzari Raymundo, Diana +11 more
openaire +3 more sources
The endoplasmic reticulum membrane protein complex (EMC) is an evolutionarily conserved, multi‐subunit transmembrane protein complex crucial to membrane protein biogenesis and cellular protein quality control. This review systematically examines the structure, functions and disease‐associated regulatory mechanisms of EMC across multiple organ systems ...
Yan Qiao +6 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 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
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
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
Hypoxic regulation of MYBL1, MEST, TCF3, TCF8, GTF2B, GTF2F2 and SNAI2 genes expression in U87 glioma cells upon IRE1 inhibition [PDF]
We investigated the impact of IRE1/ERN1 (inositol requiring enzyme 1/endoplasmic reticulum to nucleus signaling 1) knockdown on hypoxic regulation of the expression of a subset of proliferation and migration-related genes in U87 glioma cells.
O. H. Minchenko +3 more
doaj +1 more source
Abstract figure legend Mitochondria are highly dynamic organelles that continuously remodel their architecture through coordinated cycles of fusion and fission. This review examines the four key GTPases that orchestrate mitochondrial dynamics in mammals: MFN1, MFN2, OPA1, and DRP1.
Rémi Chaney +4 more
wiley +1 more source

