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
11069889 The endoribonuclease activity of mammalian IRE1 autoregulates its mRNA and is required for the unfolded protein response

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

Genes Dev 2000
16973740 The crystal structure of human IRE1 luminal domain reveals a conserved dimerization interface required for activation of the unfolded protein response

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

Proc Natl Acad Sci U S A 2006
9637683 A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells

Tirasophon, W, Welihinda, AA, Kaufman, RJ

Genes Dev 1998
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