Translocation of ATF6-alpha to the Golgi Dissociation of ATF6-alpha:BiP Complex Cleavage of ATF6-alpha by S1P Cleavage of ATF6-alpha by S2P Translocation of ATF6-alpha to the Nucleus Activation of Chaperones by ATF6-alpha ATF6-alpha is a transmembrane protein that normally resides in the Endoplasmic Reticulum (ER) membrane. Here its luminal C-terminal domain is associated with BiP, shielding 2 Golgi-targeting regions and thus keeping ATF6-alpha in the ER. Upon interaction of BiP with unfolded proteins in the ER, ATF6-alpha dissociates and transits to the Golgi where it is cleaved by the S1P and S2P proteases that reside in the Golgi, releasing the N-terminal domain of ATF6-alpha into the cytosol. After transiting to the nucleus, the N-terminal domain acts as a transcription factor to activate genes encoding chaperones. Authored: May, B, 2009-06-02 00:51:49 Edited: May, B, Gopinathrao, G, 2008-11-19 19:22:37 GENE ONTOLOGYGO:0006987 Pubmed18038217 Pubmed18048764 Pubmed18436705 Reactome Database ID Release 43381033 Reactome, http://www.reactome.org ReactomeREACT_18348 Reviewed: D'Eustachio, P, Matthews, L, Gillespie, ME, 2008-12-02 16:25:31 Reviewed: Urano, F, 2010-04-30 Activation of Chaperone Genes by ATF6-alpha PathwayStep3976 PathwayStep3977 PathwayStep3973 PathwayStep3974 PathwayStep3975 PathwayStep3983