MassIVE MSV000091745

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Structural basis for unfolded protein recognition by the ER stress-sensor IRE1alpha

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Description

ERN1/IRE1alpha is an endoplasmic reticulum sensor that recognizes misfolded proteins to activate the unfolded protein response. We used cholera toxin (CTx), which activates IRE1alpha in cells, to understand how this occurs. In vitro, the A1 subunit of CTx (CTxA1) bound the IRE1alpha lumenal domain (IRE1alphaLD). Global unfolding was not required. Instead, IRE1alphaLD recognized a 7-residue motif within a metastable region of CTxA1 that was also found in other microbial and host proteins involved in IRE1alpha activation. Binding mapped to a pocket on IRE1alphaLD normally occupied by a segment of the C-terminal flexible loop implicated in IRE1alpha regulation. Mutation of the recognition motif blocked CTx-induced IRE1alpha activation in live cells. These findings describe a mechanism for substrate recognition by IRE1alpha that induces the unfolded protein response. [doi:10.25345/C5XW4860C] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: Proximity labeling, unfolded protein response

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Principal Investigators:
(in alphabetical order) 		Steven A. Carr, Broad Institute of MIT and Harvard, United States
Submitting User: malpap1
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