Endoplasmic reticulum stress activates human IRE1α through reversible assembly of inactive dimers into small oligomers
elifesciences.org
unfolded protein response (UPR) the monomer-to-dimer transition serves as the main activation signal and that the formation of high-order oligomers is instead the primary regulatory step. an imbalance between protein folding load and capacity of the ER’s protein folding machinery IRE1 molecules asse
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- unfolded protein response (UPR)
- the monomer-to-dimer transition serves as the main activation signal and that the formation of high-order oligomers is instead the primary regulatory step.
- an imbalance between protein folding load and capacity of the ER’s protein folding machinery
- IRE1 molecules assemble into puncta in the ER membrane upon induction of ER stress
- the cooperative formation of oligomers larger than dimers plays an important role in IRE1’s enzymatic cycle.
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