Reactome | IRE1:BiP dissociates in response to unfolded protein

IRE1:BiP dissociates in response to unfolded protein

Stable Identifier

R-HSA-381217

Type

Reaction [transition]

Species

Homo sapiens

Compartment

endoplasmic reticulum membrane, endoplasmic reticulum lumen

ReviewStatus

5/5

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IRE1:BiP dissociates in response to unfolded protein

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IRE1-alpha is a single-pass transmembrane protein with a luminal N-terminus and a cytoplasmic C-terminus. IRE1-alpha is maintained in an inactive state in the Endoplasmic Reticulum (ER) membrane by interaction between the luminal domain of IRE1-alpha and the ATPase domain of BiP within the ER.
BiP is a general chaperone that also binds unfolded proteins within the ER. Thus BiP dissociates from IRE1-alpha when chaperone activity is overwhelmed by unfolded proteins in the ER.

Literature References

PubMed ID	Title	Journal	Year
19538957	Activation of mammalian IRE1alpha upon ER stress depends on dissociation of BiP rather than on direct interaction with unfolded proteins Kimata, Y, Iwawaki, T, Oikawa, D, Kohno, K	Exp Cell Res	2009
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
11897784	The protein kinase/endoribonuclease IRE1alpha that signals the unfolded protein response has a luminal N-terminal ligand-independent dimerization domain Wong, HN, Liu, CY, Kaufman, RJ, Schauerte, JA	J Biol Chem	2002

Participants

Input

Output

Participates

as an event of

IRE1alpha activates chaperones (Homo sapiens)

Authored

May, B (2009-06-02)

Reviewed

Gillespie, ME (2008-12-02)

D'Eustachio, P (2008-12-02)

Matthews, L (2008-12-02)

Urano, F (2010-04-30)

Created

May, B (2008-11-19)

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