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Membrane-tethered SCOTIN condensates elicit an endoplasmic reticulum stress response by sequestering luminal BiP

Authors
Jo, AreumJung, MinkyoMun, Ji YoungKim, Young JinYoo, Joo-Yeon
Issue Date
Feb-2025
Publisher
Cell Press
Citation
Cell Reports, v.44, no.2
Journal Title
Cell Reports
Volume
44
Number
2
URI
http://scholarworks.bwise.kr/kbri/handle/2023.sw.kbri/1245
DOI
10.1016/j.celrep.2025.115297
ISSN
2211-1247
Abstract
The endoplasmic reticulum (ER) stress response controls the balance between cellular survival and death. Here, we implicate SCOTIN, an interferon-inducible ER protein, in activating the ER stress response and modulating cell fate through its proline-rich domain (PRD)-mediated cytosolic condensation. SCOTIN over- expression leads to the formation of condensates enveloping multiple layers of the ER, accompanied by morphological signs of organelle stress. Luminal BiP chaperone proteins are sequestered within these SCOTIN condensates, which elicit ER stress responses. The colocalization of luminal BiP with SCOTIN is strictly contingent upon the PRD-mediated condensation of SCOTIN in the cytosolic compartment, closely associated with the ER membrane. The cysteine-rich domain (CRD) of SCOTIN, along with the condensation-prone PRD domain, is required for ER stress induction. We propose that membrane-associated condensation transduces signals across the ER membrane, leading to the induction of BiP assembly and the ER stress response.
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