IRE

IRE

Inositol-requiring enzyme 1 (IRE1; EC 2.7.11.1) is an endoplasmatic reticulum (ER) transmembrane sensor that activates the unfolded protein response (UPR) through a cytoplasmic kinase domain and an RNase domain to maintain the ER and cellular function. On ER stress, IRE1 RNase is activated through conformational change, autophosphorylation, and higher-order oligomerization. The active endoribonuclease domain splices XBP1 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response transcriptional activator and triggering growth arrest and apoptosis.

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More About IRE

Inositol-requiring enzyme 1 (IRE1; EC 2.7.11.1) is an endoplasmatic reticulum (ER) transmembrane sensor that activates the unfolded protein response (UPR) through a cytoplasmic kinase domain and an RNase domain to maintain the ER and cellular function[1]. On ER stress, IRE1 RNase is activated through conformational change, autophosphorylation, and higher-order oligomerization. The active endoribonuclease domain splices XBP1 mRNA to generate a new C-terminus, converting it into a potent unfolded-protein response transcriptional activator and triggering growth arrest and apoptosis[2].

[1] IRE1: ER stress sensor and cell fate executor. Y. Chen, F. Brandizzi. Trends Cell Biol. 2013, pii, S0962-8924.
[2] A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells. W. Tirasophon, A.A. Welihinda, R.J. Kaufman. Genes Dev. 1998, 12, 1812-1824.

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