Evidence map›Paper›PMID 34196665›Full record

ArticleThe Journal of cell biology2021

Cysteine cross-linking in native membranes establishes the transmembrane architecture of Ire1.

Kristina Väth, Carsten Mattes, John Reinhard, Roberto Covino, Heike Stumpf, Gerhard Hummer, Robert Ernst

Open access · hybridAbstract readVideo-Audio Media
In one paragraph

Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

8 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
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

7 authors at 2 institutions in 1 country.

Kristina Väth *Medical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, Homburg, Germany.ORCID 0000-0002-8571-6977
Carsten Mattes *Medical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, Homburg, Germany.ORCID 0000-0002-5136-706X
John Reinhard *Medical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, Homburg, Germany.ORCID 0000-0001-6363-2994
Roberto CovinoFrankfurt Institute of Advanced Sciences, Goethe-University, Frankfurt, Germany.ORCID 0000-0003-0884-0402
Heike StumpfMedical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, Homburg, Germany.ORCID 0000-0003-2515-6653
Gerhard HummerDepartment of Theoretical Biophysics, Max Planck Institute of Biophysics, Frankfurt, Germany.ORCID 0000-0001-7768-746X
Robert ErnstMedical Biochemistry and Molecular Biology, Medical Faculty, Saarland University, Homburg, Germany.ORCID 0000-0002-0283-3490
Saarland University · DEGoethe University Frankfurt · DE

Funding

European Research Council 866011
6 · The paper itself

Abstract

The ER is a key organelle of membrane biogenesis and crucial for the folding of both membrane and secretory proteins. Sensors of the unfolded protein response (UPR) monitor the unfolded protein load in the ER and convey effector functions for maintaining ER homeostasis. Aberrant compositions of the ER membrane, referred to as lipid bilayer stress, are equally potent activators of the UPR. How the distinct signals from lipid bilayer stress and unfolded proteins are processed by the conserved UPR transducer Ire1 remains unknown. Here, we have generated a functional, cysteine-less variant of Ire1 and performed systematic cysteine cross-linking experiments in native membranes to establish its transmembrane architecture in signaling-active clusters. We show that the transmembrane helices of two neighboring Ire1 molecules adopt an X-shaped configuration independent of the primary cause for ER stress. This suggests that different forms of stress converge in a common, signaling-active transmembrane architecture of Ire1.

Indexed as

Endoplasmic Reticulum StressUnfolded Protein ResponseCysteineMembrane GlycoproteinsMicroscopy, ConfocalMicroscopy, FluorescenceModels, MolecularMutationProtein Conformation, alpha-HelicalProtein FoldingProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipCysteineIRE1 protein, S cerevisiaeMembrane GlycoproteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae Proteins

Identifiers

PMID34196665
PMCPMC8256922
OpenAlexW3158887046

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.