p-S724-IRE1 dimer [endoplasmic reticulum membrane]

Stable Identifier
Homo sapiens
Locations in the PathwayBrowser

After juxtaposition of the luminal N-termini of IRE1 to form the IRE1 homodimer, the cytoplasmic C-terminal kinase domains of the IRE1 molecules associate and transphosphorylate each other's A-loop domains. This causes a change in conformation that allows binding of ADP.

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
Inferred To
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