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Chaperone BiP controls ER stress sensor Ire1 through interactions with its oligomers
Life Science Alliance 2024
Dawes, Shuravleva, et.al.
This study shows that the molecular chaperone BiP regulates the ER stress sensor Ire1 by binding directly to its oligomers: when Ire1's luminal domain engages unfolded proteins it oligomerises and exposes BiP-binding motifs, and BiP then binds these substrate-bound oligomers in an ATP-dependent way to help deactivate Ire1 once stress resolves. Flow Induced Dispersion Analysis (FIDA), on a Fida 1 instrument, was used to measure the apparent hydrodynamic radius of the Ire1 luminal domain, giving a solution readout of how substrate and BiP shift its oligomerisation, complementing NMR, microscopy and calorimetry. It is an example of using FIDA to measure protein oligomerisation and size in solution.

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Chaperone BiP controls ER stress sensor Ire1 through interactions with its oligomers
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