Evidence map›Paper›PMID 38714852›Full record

ArticleNature cell biology2024

Mammalian IRE1α dynamically and functionally coalesces with stress granules.

Songzi Liu, Xiaoge Zhang, Xin Yao, Guan Wang, Shijia Huang, Peng Chen, Mingliang Tang, Jie Cai, Zhuyin Wu, Yiliang Zhang and 9 more

Abstract read
PubMed Publisher
In one paragraph

Article in Nature cell biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

41 citing papers in PubMed.

  1. Review
  2. Prion-Like Protein LENG8-Mediated Nucleation Drives Stress Granule Assembly.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. Metabolites · 2026
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. The Role of Stress Granules in Cardiovascular Diseases.Reviews in cardiovascular medicine · 2026
    Review
  10. Boosting ribosomal translationBioactive materials · 2026
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Article
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

19 authors.

Songzi Liu *Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences; TaiKang Center for Life and Medical Sciences; the Institute for Advanced Studies; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China.
Xiaoge Zhang *Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences; TaiKang Center for Life and Medical Sciences; the Institute for Advanced Studies; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China.
Xin Yao *Hubei Key Laboratory of Cell Homeostasis, College of Life Sciences; TaiKang Center for Life and Medical Sciences; the Institute for Advanced Studies; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China.
Guan WangComprehensive Cancer Center, Beckman Research Institute, City of Hope Medical Center, Duarte, CA, USA.
Shijia HuangHubei Key Laboratory of Cell Homeostasis, College of Life Sciences; TaiKang Center for Life and Medical Sciences; the Institute for Advanced Studies; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China.
Peng ChenHubei Key Laboratory of Cell Homeostasis, College of Life Sciences; TaiKang Center for Life and Medical Sciences; the Institute for Advanced Studies; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China.
Mingliang TangHubei Key Laboratory of Cell Homeostasis, College of Life Sciences; TaiKang Center for Life and Medical Sciences; the Institute for Advanced Studies; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China.
Jie CaiHubei Key Laboratory of Cell Homeostasis, College of Life Sciences; TaiKang Center for Life and Medical Sciences; the Institute for Advanced Studies; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China.
Zhuyin WuHubei Key Laboratory of Cell Homeostasis, College of Life Sciences; TaiKang Center for Life and Medical Sciences; the Institute for Advanced Studies; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China.
Yiliang ZhangHubei Key Laboratory of Cell Homeostasis, College of Life Sciences; TaiKang Center for Life and Medical Sciences; the Institute for Advanced Studies; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China.
Rongzhi XuHubei Key Laboratory of Cell Homeostasis, College of Life Sciences; TaiKang Center for Life and Medical Sciences; the Institute for Advanced Studies; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China.
Kai LiuHubei Key Laboratory of Cell Homeostasis, College of Life Sciences; TaiKang Center for Life and Medical Sciences; the Institute for Advanced Studies; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China.
Kangmin HeState Key Laboratory of Molecular Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, China.
Yan WangHubei Key Laboratory of Cell Homeostasis, College of Life Sciences; TaiKang Center for Life and Medical Sciences; the Institute for Advanced Studies; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China.ORCID http://orcid.org/0000-0002-3561-3021
Lei JiangComprehensive Cancer Center, Beckman Research Institute, City of Hope Medical Center, Duarte, CA, USA.ORCID http://orcid.org/0000-0002-8596-556X
Qiong A WangComprehensive Cancer Center, Beckman Research Institute, City of Hope Medical Center, Duarte, CA, USA.ORCID http://orcid.org/0000-0003-2224-4287
Liangyou RuiDepartment of Molecular and Integrative Physiology, the University of Michigan Medical School, Ann Arbor, MI, USA.ORCID http://orcid.org/0000-0001-8433-8137
Jianmiao LiuCellular Signaling Laboratory, Key Laboratory of Molecular Biophysics of Ministry of Education, Huazhong University of Science and Technology, Wuhan, China.
Yong LiuHubei Key Laboratory of Cell Homeostasis, College of Life Sciences; TaiKang Center for Life and Medical Sciences; the Institute for Advanced Studies; Frontier Science Center for Immunology and Metabolism, Wuhan University, Wuhan, China. liuyong31279@whu.edu.cn.ORCID http://orcid.org/0000-0001-7771-4181

Funding

National Natural Science Foundation of China (National Science Foundation of China) 32021003National Natural Science Foundation of China (National Science Foundation of China) 323B1006National Natural Science Foundation of China (National Science Foundation of China) 82230026National Natural Science Foundation of China (National Science Foundation of China) 91857204National Natural Science Foundation of China (National Science Foundation of China) 92357307
6 · The paper itself

Abstract

Upon endoplasmic reticulum (ER) stress, activation of the ER-resident transmembrane protein kinase/endoribonuclease inositol-requiring enzyme 1 (IRE1) initiates a key branch of the unfolded protein response (UPR) through unconventional splicing generation of the transcription factor X-box-binding protein 1 (XBP1s). Activated IRE1 can form large clusters/foci, whose exact dynamic architectures and functional properties remain largely elusive. Here we report that, in mammalian cells, formation of IRE1α clusters is an ER membrane-bound phase separation event that is coupled to the assembly of stress granules (SGs). In response to different stressors, IRE1α clusters are dynamically tethered to SGs at the ER. The cytosolic linker portion of IRE1α possesses intrinsically disordered regions and is essential for its condensation with SGs. Furthermore, disruption of SG assembly abolishes IRE1α clustering and compromises XBP1 mRNA splicing, and such IRE1α-SG coalescence engenders enrichment of the biochemical components of the pro-survival IRE1α-XBP1 pathway during ER stress. Our findings unravel a phase transition mechanism for the spatiotemporal assembly of IRE1α-SG condensates to establish a more efficient IRE1α machinery, thus enabling higher stress-handling capacity.

Indexed as

Endoplasmic Reticulum StressEndoribonucleasesProtein Serine-Threonine KinasesX-Box Binding Protein 1AnimalsCytoplasmic GranulesDNA-Binding ProteinsEndoplasmic ReticulumHeLa CellsHumansMiceRegulatory Factor X Transcription FactorsRNA SplicingSignal TransductionStress GranulesTranscription FactorsDNA-Binding ProteinsEndoribonucleasesERN1 protein, humanProtein Serine-Threonine KinasesRegulatory Factor X Transcription FactorsTranscription FactorsX-Box Binding Protein 1XBP1 protein, humanXbp1 protein, mouse

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.