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.

Stress sensors in the membrane of the endoplasmic reticulum respond to the accumulation of unfolded proteins by briefly forming small phosphorylation-competent oligomers and dissolving back into active dimers.

The unfolded protein response sensor/transducer IRE1-mediated splicing of XBP1 mRNA encoding its active downstream transcription factor to maintain the homeostasis of the endoplasmic reticulum is sufficient for growth and development of medaka fish.

Development of a live single-molecule imaging approach to visualize XBP1 mRNAs, which are recruited for translation on the ER and efficiently spliced in the absence of large IRE1α foci.

Client protein-driven reversal of endoplasmic reticulum chaperone (BiP) mediated-repression is revealed as a principal component of the regulation of the unfolded protein response transducer IRE1 in cells.

The IRE1/XBP1 signaling in myofibers is essential for robust skeletal muscle regeneration in response to injury.

Quantitative FRET UPR induction assay is used to measure IRE1 and BIP association and dissociation by a variety of ER misfolded proteins and by an important BiP substrate-binding domain mutant, significantly enhancing the evidence for the allosteric UPR induction model.

Building on previous work (Plumb et al., 2015), it is shown that the Sec61 translocon controls the oligomerization, activation and inactivation of Ire1α during endoplasmic reticulum stress.

Estrogen is a systemic factor that promotes hematopoietic regeneration by activating the unfolded protein responses.

A whole-genome siRNA screen identifies ICE1 as a factor required for accurate sensing and quality control of mRNAs containing premature stop codons.