Death receptor 5 can directly sense misfolded proteins downstream of the endoplasmic reticulum to provide a quality control mechanism that executes apoptosis and prevents further production of misfolded proteins.
Rolf M Schmidt, Julia P Schessner ... Sebastian Schuck
Endoplasmic reticulum stress in yeast activates not only the UPR but also Rpn4, promoting the clearance of misfolded proteins from the cytosol as part of a modular cross-compartment stress response.
G Elif Karagöz, Diego Acosta-Alvear ... Peter Walter
ER-stress sensing mechanism of the unfolded protein response sensor/transducer IRE1 is conserved from yeast to mammals, where in mammals, unfolded protein binding to IRE1's ER lumenal domain is coupled to its oligomerization and activation through an allosteric conformational change.
Gregory M Solis, Rozina Kardakaris ... Michael Petrascheck
Directly targeting the ribosome to attenuate translation partly mimics the integrated stress response, increasing lifespan and preserving protein folding capacity even in older individuals with dysfunctional stress response signaling.
Direct modification by endogenous peroxide of a conserved cysteine in the molecular chaperone BiP decouples its ATPase and peptide-binding activities, allowing for enhanced polypeptide holdase activity during oxidative stress.
Wouter Huiting, Suzanne L Dekker ... Steven Bergink
Various genotoxic stresses trigger widespread aggregation of abundant, liquid-liquid phase separation-prone proteins, suggesting that genotoxic stress is a potential driver of disease-associated protein aggregation.
Benoît Landrein, Annamaria Kiss ... Olivier Hamant
Mechanical stress promotes the expression of the homeobox gene and meristem master regulator STM, synergistically and independently from auxin depletion.
Avihu H Yona, Zohar Bloom-Ackermann ... Yitzhak Pilpel
Experimental evolution and systematic sequence analysis of transfer RNA genes reveal that anticodon mutations provide adaptive plasticity to the translation machinery.
The envelope stress factor DolP associates with the outer membrane protein assembly machinery and supports proper folding and functioning of BamA contributing to preserve envelope integrity.