Preferred Name | Dissociation of ATF6-alpha:BiP Complex | |
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Definitions |
Reviewed: D'Eustachio, P, Matthews, L, Gillespie, ME, 2008-12-02 16:25:31 Reviewed: Urano, F, 2010-04-30 Authored: May, B, 2009-06-02 00:51:49 Edited: May, B, 2009-06-02 00:51:49 ATF6-alpha is a transmembrane protein located in the endoplasmic reticulum (ER) membrane with N-terminal cytoplasmic and C-terminal luminal domains. BiP binds the luminal domain of ATF6-alpha via the substrate binding domain of BiP. Binding of BiP blocks 2 Golgi localization sequences on ATF6-alpha, maintaining ATF6-alpha in the ER. <br> BiP is also a general chaperone capable of binding unfolded proteins in the ER lumen. When chaperone activity in the ER is overwhelmed, BiP dissociates from ATF6-alpha and binds the excess unfolded proteins. It is unclear whether the dissociation is due to competition of unfolded proteins for BiP or to a more specific interaction between BiP and ATF6-alpha. The dissociation exposes the Golgi localization sequences of ATF6-alpha and allows ATF6-alpha to transit to the Golgi. |
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http://purl.obolibrary.org/obo/HINO_0008862 |
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comment |
Reviewed: D'Eustachio, P, Matthews, L, Gillespie, ME, 2008-12-02 16:25:31 Reviewed: Urano, F, 2010-04-30 Authored: May, B, 2009-06-02 00:51:49 Edited: May, B, 2009-06-02 00:51:49 ATF6-alpha is a transmembrane protein located in the endoplasmic reticulum (ER) membrane with N-terminal cytoplasmic and C-terminal luminal domains. BiP binds the luminal domain of ATF6-alpha via the substrate binding domain of BiP. Binding of BiP blocks 2 Golgi localization sequences on ATF6-alpha, maintaining ATF6-alpha in the ER. |
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definition source |
Pubmed12110171 Reactome, http://www.reactome.org Pubmed15657421 Pubmed11821395 |
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label |
Dissociation of ATF6-alpha:BiP Complex |
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prefixIRI |
HINO:0008862 |
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prefLabel |
Dissociation of ATF6-alpha:BiP Complex |
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seeAlso |
Reactome Database ID Release 43381158 ReactomeREACT_18323 |
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subClassOf |