IRE1 Antibody

1. The most conserved transducer of ER stress, Ire1, uses an amphipathic helix to sense membrane aberrancies and control unfolded protein response activity. PMID: 28689662
2. Here we show that in yeast cells, the ER-stress sensor Ire1 was activated upon zinc deficiency PMID: 23748779
3. Under ER stress, Ire1 molecules exist in activated and Bip-associated state. PMID: 23387983
4. Results show that the kinase domain autophosphorylatse the auto-inhibitory region in order to relieve auto-inhibition and that ADP acts as a switch to activate the kinase extension nuclease domain-catalyzed HAC1 mRNA cleavage. PMID: 23541589
5. the cytosolic or transmembrane domain of Ire1 senses membrane aberrancy PMID: 21775630
6. core ER-lumenal domain (cLD) of Ire1 binds to unfolded proteins in yeast and to peptides in vitro; peptide binding caused Ire1 cLD oligomerization in vitro, suggesting direct binding to unfolded proteins activates unfolded protein response PMID: 21852455
7. Flavonol activation defines an unanticipated ligand-binding site in the kinase-RNase domain of IRE1. PMID: 20417606
8. although its sequence is little conserved evolutionarily, subregion IV plays an essential role to promote Ire1 dimer formation PMID: 15954865
9. Our results are consistent with de-phosphorylation of Ire1 being a mechanism for antagonizing UPR signalling. PMID: 16990850
10. The capacity of a highly basic sequence in the linker region of Ire1p to function as a nuclear localization sequence (NLS) both in vivo and in vitro, was analyzed. PMID: 17035634
11. Observations indicate that in addition to BiP dissociation and self-association of Ire1, another unknown change on the luminal side is crucial for Ire1 activation. PMID: 17452628
12. Upon endoplasmic reticulum (ER) stress, Ire1 clusters and actually interacts with unfolded proteins. PMID: 17923530
13. We have determined the crystal structure of the dual catalytic region of Ire1at 2.4 A resolution, revealing the fusion of a domain, which we term the KEN domain, to the protein kinase domain. PMID: 18191223
14. oligomerization is central to Ire1 function and is an intrinsic attribute of its cytosolic domains; 3.2-A crystal structure of the oligomer of the Ire1 cytosolic domains in complex with a kinase inhibitor PMID: 19079236

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KEGG: sce:YHR079C

STRING: 4932.YHR079C