Publication details for Dr Martin SchröderM. E. Schröder & R. J. Kaufman (2007). Ire1. UCSD-Nature Molecule Pages
- Publication type: Journal Article
- ISSN/ISBN: 1477-5921
- DOI: 10.1038/mp.a003134.01
- Keywords: Ire1, unfolded protein response, endoplasmic reticulum
- Further publication details on publisher web site
Author(s) from Durham
Inositol-requiring 1 (IRE1), also known as endoplasmic reticulum (ER) to nucleus signaling 1 (ERN1), is a proximal sensor for the status of ER luminal protein folding in a stress response called the unfolded protein response (UPR). When unfolded proteins accumulate in the ER, a stress situation referred to as ‘ER stress’ ensues. IRE1 regulates adaptive, inflammatory and apoptotic responses to this stress situation. The UPR is critical for the development and normal function of secretory cell types, nutrient sensing, biogenesis of the ER. The UPR plays important roles in numerous human diseases caused by protein misfolding and retention in the ER, organismal responses to infections, and many physiological and pathophysiological conditions, such as ageing, behavioral stress, exposure to chemicals, obesity and sleep deprivation. This molecule page reviews our current knowledge about the activation and regulation of IRE1, and the signaling mechanisms initiated by it.