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IRE1 inhibitors block inositol-requiring enzyme 1 (IRE1), a sensor of endoplasmic reticulum stress. In 1993, yeast IRE1 was identified as a transmembrane protein kinase required to induce genes for endoplasmic reticulum resident proteins. The enzyme couples a cytosolic kinase domain to an endoribonuclease (RNase) domain. Studies in 2001 and 2002 showed that IRE1 splices X-box binding protein 1 (XBP1) mRNA, producing an active transcription factor of the unfolded protein response. 4μ8C, STF-083010 and MKC8866 inhibit the RNase activity of IRE1α. KIRA6 and Kira8 bind the kinase site and suppress RNase activity allosterically, whereas APY29 is an ATP-competitive ligand of the kinase domain.
DSA8 is an IRE1 RNase modulator that functions as a type II kinase inhibitor. It is an effective tool for studying pathways involved in cancer and metabolic diseases, including diabetes. DSA8's ability to modulate IRE1 activity makes it valuable for investigating the unfolded protein response and its implications in various diseases.
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