Reactome | IRE1 dimer autophosphorylates

IRE1 dimer autophosphorylates

Stable Identifier

R-HSA-381091

Type

Reaction [transition]

Species

Homo sapiens

Compartment

endoplasmic reticulum membrane, cytosol

ReviewStatus

5/5

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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