IRE1 dimer autophosphorylates

Stable Identifier
Reaction [transition]
Homo sapiens
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Dimerization of the N-terminal luminal regions of IRE1-alpha brings the cytosolic C-terminal regions in proximity. The C-terminal region possesses kinase activity and the homodimer trans-autophosphorylates. From homology with Saccharomyces IRE1-alpha the phosphorylation of human IRE1-alpha is believed to be at Ser724.

Literature References
PubMed ID Title Journal Year
16973740 The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response

Back, SH, Liu, CY, Kaufman, RJ, Peisach, D, Zhou, J, Xu, Z, Clark, RL

Proc Natl Acad Sci U S A 2006
11069889 The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response

Lee, K, Kaufman, RJ, Callaghan, B, Welihinda, A, Tirasophon, W

Genes Dev 2000
9637683 A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells

Kaufman, RJ, Welihinda, AA, Tirasophon, W

Genes Dev 1998
Catalyst Activity

protein serine/threonine kinase activity of IRE1 dimer [endoplasmic reticulum membrane]

Orthologous Events
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