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The UPRosome-decoding novel biological outputs of IRE1 alpha function
(Company Biologists, 2020)
Different perturbations alter the function of the endoplasmic reticulum (ER), resulting in the accumulation of misfolded proteins in its lumen, a condition termed ER stress. To restore ER proteostasis, a highly conserved ...
Non-canonical function of IRE1 alpha determines mitochondria-associated endoplasmic reticulum composition to control calcium transfer and bioenergetics
(2019)
Mitochondria-associated membranes (MAMs) are central microdomains that fine-tune bioenergetics by the local transfer of calcium from the endoplasmic reticulum to the mitochondrial matrix. Here, we report an unexpected ...
IRE1 alpha governs cytoskeleton remodelling and cell migration through a direct interaction with filamin A
(2018)
Maintenance of endoplasmic reticulum (ER) proteostasis is controlled by a signalling network known as the unfolded protein response (UPR). Here, we identified filamin A as a major binding partner of the ER stress transducer ...
IRE1 alpha governs cytoskeleton remodelling and cell migration through a direct interaction with filamin A
(2018)
Maintenance of endoplasmic reticulum (ER) proteostasis is controlled by a signalling network known as the unfolded protein response (UPR). Here, we identified filamin A as a major binding partner of the ER stress transducer ...
Dual IRE1 RNase functions dictate glioblastoma development
(Wiley, 2018)
Proteostasis imbalance is emerging as a major hallmark of cancer, driving tumor aggressiveness. Evidence suggests that the endoplasmic reticulum (ER), a major site for protein folding and quality control, plays a critical ...
Interactome screening identifies the ER luminal chaperone Hsp47 as a regulator of the unfolded protein response transducer IRE1 alpha
(Cell Press, 2018)
Maintenance of endoplasmic reticulum (ER) proteostasis is controlled by a dynamic signaling network known as the unfolded protein response (UPR). IRE1a is a major UPR transducer, determining cell fate under ER stress. We ...
The unfolded protein response and cell fate control
(Cell Press, 2018)
The secretory capacity of a cell is constantly challenged by physiological demands and pathological perturbations. To adjust and match the protein-folding capacity of the endoplasmic reticulum (ER) to changing secretory ...
IRE1 alpha governs cytoskeleton remodelling and cell migration through a direct interaction with filamin A
(Nature, 2018)
Maintenance of endoplasmic reticulum (ER) proteostasis is controlled by a signalling network known as the unfolded protein response (UPR). Here, we identified filamin A as a major binding partner of the ER stress transducer ...
PERK regulated miR-424(322)-503 cluster fine-tunes activation of IRE1 and ATF6 during Unfolded Protein Response
(Nature, 2015)
The endoplasmic reticulum (ER) responds to changes in intracellular homeostasis through activation of the unfolded protein response (UPR). UPR can facilitate the restoration of cellular homeostasis, via the concerted ...
Genotoxic stress triggers the activation of IRE1 alpha-dependent RNA decay to modulate the DNA damage response
(Nature, 2020)
The molecular connections between homeostatic systems that maintain both genome integrity and proteostasis are poorly understood. Here we identify the selective activation of the unfolded protein response transducer IRE1 ...