Evidence map›Paper›PMID 23839788›Full record

ArticleThe Plant cell2013

Arabidopsis CURVATURE THYLAKOID1 proteins modify thylakoid architecture by inducing membrane curvature.

Ute Armbruster, Mathias Labs, Mathias Pribil, Stefania Viola, Wenteng Xu, Michael Scharfenberg, Alexander P Hertle, Ulrike Rojahn, Poul Erik Jensen, Fabrice Rappaport and 4 more

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 141 papers.

0numbers the graph read from it
0cells of the map it votes in
141citing papers in PubMed
9.3field-weighted citation impact, top 1% 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

141 citing papers in PubMed, 277 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. The pathogenic effector PHYL1The Plant journal : for cell and molecular biology · 2026
    Article
  6. VIA1 is a conserved regulator of thylakoid membrane integrity that acts through VIPP1.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Article
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  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Article
  19. Review
  20. Article

81 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

14 authors at 5 institutions in 4 countries.

Ute ArmbrusterPlant Molecular Biology (Botany), Department Biology I, Ludwig-Maximilians-Universität München, 81252 Planegg-Martinsried, Germany.
Mathias Labs
Mathias Pribil
Stefania Viola
Wenteng Xu
Michael Scharfenberg
Alexander P Hertle
Ulrike Rojahn
Poul Erik Jensen
Fabrice Rappaport
Pierre Joliot
Peter Dörmann
Gerhard Wanner
Dario Leister
Ludwig-Maximilians-Universität München · DEInstitut de Biologie Physico-Chimique · FRUniversity of Bonn · DEUniversity of Copenhagen · DKUniversity of Trento · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chloroplasts of land plants characteristically contain grana, cylindrical stacks of thylakoid membranes. A granum consists of a core of appressed membranes, two stroma-exposed end membranes, and margins, which connect pairs of grana membranes at their lumenal sides. Multiple forces contribute to grana stacking, but it is not known how the extreme curvature at margins is generated and maintained. We report the identification of the CURVATURE THYLAKOID1 (CURT1) protein family, conserved in plants and cyanobacteria. The four Arabidopsis thaliana CURT1 proteins (CURT1A, B, C, and D) oligomerize and are highly enriched at grana margins. Grana architecture is correlated with the CURT1 protein level, ranging from flat lobe-like thylakoids with considerably fewer grana margins in plants without CURT1 proteins to an increased number of membrane layers (and margins) in grana at the expense of grana diameter in overexpressors of CURT1A. The endogenous CURT1 protein in the cyanobacterium Synechocystis sp PCC6803 can be partially replaced by its Arabidopsis counterpart, indicating that the function of CURT1 proteins is evolutionary conserved. In vitro, Arabidopsis CURT1A proteins oligomerize and induce tubulation of liposomes, implying that CURT1 proteins suffice to induce membrane curvature. We therefore propose that CURT1 proteins modify thylakoid architecture by inducing membrane curvature at grana margins.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsChlorophyllChloroplastsImmunoblottingIntracellular MembranesLipidsMicroscopy, Electron, ScanningMicroscopy, Electron, TransmissionMolecular Sequence DataMutationPhosphorylationPhotosynthesisPhylogenyPlant LeavesArabidopsis ProteinsChlorophyllLipidsProteolipidsproteoliposomes

Identifiers

PMID23839788
PMCPMC3753390
OpenAlexW2164188684

What OpenQuestion holds

Textmetadata
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.