Proteomics

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Calcium-mediated calreticulin IRE1α interaction drives dynamic fluctuation of IRE1α activity under chronic endoplasmic reticulum stress

ABSTRACT: To investigate the mechanisms underlying fluctuating IRE1α phosphorylation under chronic endoplasmic reticulum stress, we performed co-immunoprecipitation coupled with mass spectrometry (IP-MS) to identify IRE1α-interacting proteins. Protein complexes were analyzed by LC-MS/MS, followed by bioinformatic enrichment analysis to identify candidate regulators of IRE1α phosphorylation and activity.

ORGANISM(S): Homo Sapiens

SUBMITTER: Likun Wang  

PROVIDER: PXD073899 | iProX | Fri Jan 30 00:00:00 GMT 2026

REPOSITORIES: iProX

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Calcium-mediated calreticulin-IRE1α interaction drives dynamic fluctuation of IRE1α activity under chronic endoplasmic reticulum stress.

Cao Jianwei J   Zhao Xudong X   Xu Yunxin Y   Yang Chen C   Huo Yazhen Y   Li Ting T   Gu Wenjia W   Wang Lei L   Wang Youjun Y   Wang Likun L  

Nature communications 20260317 1

The unfolded protein response (UPR) triggered by endoplasmic reticulum (ER) stress can be both pro-survival or pro-apoptotic, depending on the duration and intensity of the stress. ER stress under (patho)physiological conditions can last for long time, yet the dynamic regulation of the UPR under prolong ER stress is largely unknown. Here, we characterized the UPR dynamics during pharmacologically induced long-term ER stress and revealed an "up-down-up" fluctuation pattern of the IRE1α signal in  ...[more]

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