Evidence map›Paper›PMID 17923530›Full record

ArticleThe Journal of cell biology2007

Two regulatory steps of ER-stress sensor Ire1 involving its cluster formation and interaction with unfolded proteins.

Yukio Kimata, Yuki Ishiwata-Kimata, Tatsuhiko Ito, Aiko Hirata, Tomohide Suzuki, Daisuke Oikawa, Masato Takeuchi, Kenji Kohno

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 145 papers.

0numbers the graph read from it
0cells of the map it votes in
145citing papers in PubMed
5.6field-weighted citation impact, top 3% of its field
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

145 citing papers in PubMed, 297 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Review
  12. Review
  13. Review
  14. Unfolded protein response and angiogenesis in malignancies.Biochimica et biophysica acta. Reviews on cancer · 2023
    Review
  15. Article
  16. Diverse Sphingolipid Species Harbor Different Effects on Ire1 Clustering.International journal of molecular sciences · 2022
    Article
  17. Article
  18. Article
  19. Article
  20. The role of cellular proteostasis in antitumor immunity.The Journal of biological chemistry · 2022
    Review

85 more citing papers are in PubMed but not listed here.

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

8 authors at 2 institutions in 1 country.

Yukio KimataGraduate School of Biological Sciences, Nara Institute of Science and Technology, Ikoma, Nara 630-0192, Japan. kimata@zero.ad.jp
Yuki Ishiwata-Kimata
Tatsuhiko Ito
Aiko Hirata
Tomohide Suzuki
Daisuke Oikawa
Masato Takeuchi
Kenji Kohno
Nara Institute of Science and Technology · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chaperone protein BiP binds to Ire1 and dissociates in response to endoplasmic reticulum (ER) stress. However, it remains unclear how the signal transducer Ire1 senses ER stress and is subsequently activated. The crystal structure of the core stress-sensing region (CSSR) of yeast Ire1 luminal domain led to the controversial suggestion that the molecule can bind to unfolded proteins. We demonstrate that, upon ER stress, Ire1 clusters and actually interacts with unfolded proteins. Ire1 mutations that affect these phenomena reveal that Ire1 is activated via two steps, both of which are ER stress regulated, albeit in different ways. In the first step, BiP dissociation from Ire1 leads to its cluster formation. In the second step, direct interaction of unfolded proteins with the CSSR orients the cytosolic effector domains of clustered Ire1 molecules.

Indexed as

Protein FoldingEndoplasmic ReticulumEnzyme ActivationFungal ProteinsHSP70 Heat-Shock ProteinsMembrane GlycoproteinsModels, BiologicalProtein Serine-Threonine KinasesSaccharomyces cerevisiae ProteinsFungal ProteinsHSP70 Heat-Shock ProteinsIRE1 protein, S cerevisiaeKAR2 protein, yeastMembrane GlycoproteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae Proteins

Identifiers

PMID17923530
PMCPMC2064738
OpenAlexW2111587627

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

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.