title: IRE1: ER stress sensor and cell fate executor.
abstract: Cells operate a signaling network termed the unfolded protein response (UPR) to monitor protein-folding capacity in the endoplasmic reticulum (ER). Inositol-requiring enzyme 1 (IRE1) is an ER transmembrane sensor that activates the UPR to maintain the ER and cellular function. Although mammalian IRE1 promotes cell survival, it can initiate apoptosis via decay of antiapoptotic miRNAs. Convergent and divergent IRE1 characteristics between plants and animals underscore its significance in cellular homeostasis. This review provides an updated scenario of the IRE1 signaling model, discusses emerging IRE1 sensing mechanisms, compares IRE1 features among species, and outlines exciting future directions in UPR research.
authors.affiliation: MSU-DOE Plant Research Laboratory and Department of Plant Biology, Michigan State University, 612 Wilson Rd, Room 122, East Lansing, MI 48824, USA.
authors.forename: Yani
authors.initials: Y
authors.lastname: Chen
authors.forename: Federica
authors.initials: F
authors.lastname: Brandizzi
mesh_terms: D004721:Endoplasmic Reticulum / Q000201:enzymology* / Q000378:metabolism*; D059865:Endoplasmic Reticulum Stress; D004722:Endoribonucleases / Q000378:metabolism*; D006801:Humans; D008954:Models, Biological; D017346:Protein Serine-Threonine Kinases / Q000378:metabolism*; D015398:Signal Transduction
chemical_list: C528229:ERN1 protein, human; D017346:Protein Serine-Threonine Kinases; D004722:Endoribonucleases
keywords: ER stress; IRE1; cell fate; membrane trafficking system; protein quality control; unfolded protein response