IRE1 dimer autophosphorylates

Stable Identifier
R-HSA-381091
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
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
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
protein serine/threonine kinase activity of IRE1 dimer [endoplasmic reticulum membrane]
Physical Entity
Activity
Orthologous Events
Authored
Reviewed
Created
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