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TitleA structural basis for chaperone repression of stress signaling from the endoplasmic reticulum.
Journal, issue, pagesMol Cell, Vol. 85, Issue 21, Page 4047-44063.e7, Year 2025
Publish dateNov 6, 2025
AuthorsLisa Neidhardt / Joanne Tung / Miriam Kuchersky / Jakub Milczarek / Vasileios Kargas / Katherine Stott / Rina Rosenzweig / David Ron / Yahui Yan /
PubMed AbstractThe endoplasmic reticulum (ER) unfolded protein response (UPR) is tuned by the balance between unfolded proteins and chaperones. Reserve chaperones suppress UPR transducers via their stress-sensing ...The endoplasmic reticulum (ER) unfolded protein response (UPR) is tuned by the balance between unfolded proteins and chaperones. Reserve chaperones suppress UPR transducers via their stress-sensing luminal domains, but the underlying mechanisms remain unclear. The ER chaperone AGR2 is known to repress the UPR transducer IRE1β. Here, structural prediction, X-ray crystallography, and NMR spectroscopy identify critical interactions between an AGR2 monomer and a regulatory loop in IRE1β's luminal domain. However, in the repressive complex, it is an AGR2 dimer that binds IRE1β. Cryoelectron microscopy (cryo-EM) reconstruction explains this feature: one AGR2 protomer engages the regulatory loop, while the second asymmetrically binds IRE1β's luminal domain's C terminus, blocking IRE1β-activating dimerization. Molecular dynamic simulations indicate that the second, disruptive AGR2 protomer exploits rare fluctuations in the IRE1β dimer that expose its binding site. Thus, AGR2 disrupts IRE1β dimers to suppress the UPR, priming the system for activation by chaperone clients that compete for AGR2.
External linksMol Cell / PubMed:41135511
MethodsEM (single particle) / X-ray diffraction
Resolution1.9 - 4.1 Å
Structure data

52616

9i3u

EMDB-52616, PDB-9i3u:
Cryo-EM structure of the AGR2 dimer in complex with the monomeric IRE1beta luminal domain
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-52618: A cryo-EM map for two copies of IRE1beta-(AGR2)2 trimer
Method: EM (single particle) / Resolution: 4.1 Å

PDB-9i3f:
Crystal structure of the AGR2 and IRE1beta_loop complex
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
KeywordsCHAPERONE / molecular chaperones / unfolded protein response (UPR) / endoplasmic reticulum (ER) / protein multimerisation / endoplasmic reticulum (ER) / molecular chaperones/ protein multimerisation/ unfolded protein response (UPR)

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