Dissociation of IRE1:BiP heterodimer

Reviewed: D'Eustachio, P, Matthews, L, Gillespie, ME, 2008-12-02 16:25:31 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. <br>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. Reviewed: Urano, F, 2010-04-30 Authored: May, B, 2009-06-02 00:51:49 Edited: May, B, 2009-06-02 00:51:49

http://purl.obolibrary.org/obo/HINO_0008881

Reviewed: D'Eustachio, P, Matthews, L, Gillespie, ME, 2008-12-02 16:25:31

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.

Reviewed: Urano, F, 2010-04-30

Authored: May, B, 2009-06-02 00:51:49

Edited: May, B, 2009-06-02 00:51:49

Pubmed16973740

Pubmed19538957

Reactome, http://www.reactome.org

Pubmed11897784

http://purl.obolibrary.org/obo/HINO_0017507

http://purl.obolibrary.org/obo/HINO_0008737

http://purl.obolibrary.org/obo/HINO_0017506

http://purl.obolibrary.org/obo/UniProt_O75460

Dissociation of IRE1:BiP heterodimer

HINO:0008881

Dissociation of IRE1:BiP heterodimer

ReactomeREACT_18294

Reactome Database ID Release 43381217

http://purl.obolibrary.org/obo/INO_0000040