Evidence map›Paper›PMID 17599066›Full record

ArticleThe EMBO journal2007

The Caenorhabditis elegans septin complex is nonpolar.

Corinne M John, Richard K Hite, Christine S Weirich, Daniel J Fitzgerald, Hatim Jawhari, Mahamadou Faty, Dominik Schläpfer, Ruth Kroschewski, Fritz K Winkler, Tom Walz and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

76 citing papers in PubMed, 158 citations in OpenAlex.

  1. TaggingbioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Animal septins contain functional transmembrane domains.bioRxiv : the preprint server for biology · 2025
    Article
  4. Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  5. The Roles of Septins in Regulating Fission Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  6. Article
  7. Curvature sensing as an emergent property of multiscale assembly of septins.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  8. Article
  9. Article
  10. Article
  11. Septins, a cytoskeletal protein family, with emerging role in striated muscle.Journal of muscle research and cell motility · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Septins From Protists to People.Frontiers in cell and developmental biology · 2021
    Review
  16. Review
  17. The Structural Biology of Septins and Their Filaments: An Update.Frontiers in cell and developmental biology · 2021
    Review
  18. Article
  19. Article
  20. Review

16 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

12 authors at 3 institutions in 2 countries.

Corinne M JohnInstitute of Biochemistry, ETH Zürich, Zürich, Switzerland.
Richard K Hite
Christine S Weirich
Daniel J Fitzgerald
Hatim Jawhari
Mahamadou Faty
Dominik Schläpfer
Ruth Kroschewski
Fritz K Winkler
Tom Walz
Yves Barral
Michel O Steinmetz
ETH Zurich · CHPaul Scherrer Institute · CHHarvard University · US

Funding

Single particle reconstructionP01GM062580 · NIGMS · HARVARD MEDICAL SCHOOL · PI HARRISON, STEPHEN COPLAN · 2001 to 2016
$23.7M
MOLECULAR BIOLOGY OF TISSUE AND ORGAN DEVELOPMENTT32HD007390 · NICHD · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI OLSEN, BJORN REINO · 1990 to 2004
$957k
NICHD NIH HHS 5T32HD007390NICHD NIH HHS T32 HD007390NIGMS NIH HHS GM62580NIGMS NIH HHS P01 GM062580
6 · The paper itself

Abstract

Septins are conserved GTPases that form heteromultimeric complexes and assemble into filaments that play a critical role in cell division and polarity. Results from budding and fission yeast indicate that septin complexes form around a tetrameric core. However, the molecular structure of the core and its influence on the polarity of septin complexes and filaments is poorly defined. The septin complex of the nematode Caenorhabditis elegans is formed entirely by the core septins UNC-59 and UNC-61. We show that UNC-59 and UNC-61 form a dimer of coiled-coil-mediated heterodimers. By electron microscopy, this heterotetramer appears as a linear arrangement of four densities representing the four septin subunits. Fusion of GFP to the N termini of UNC-59 and UNC-61 and subsequent electron microscopic visualization suggests that the sequence of septin subunits is UNC-59/UNC-61/UNC-61/UNC-59. Visualization of GFP extensions fused to the extremity of the C-terminal coiled coils indicates that these extend laterally from the heterotetrameric core. Together, our study establishes that the septin core complex is symmetric, and suggests that septins form nonpolar filaments.

Indexed as

AnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsCell Cycle ProteinsChromatography, GelDimerizationGTP-Binding ProteinsHydrophobic and Hydrophilic InteractionsInsectaModels, BiologicalMultiprotein ComplexesProtein Structure, QuaternaryProtein Structure, SecondaryProtein SubunitsProtein TransportYeastsCaenorhabditis elegans ProteinsCell Cycle ProteinsGTP-Binding ProteinsMultiprotein ComplexesProtein SubunitsUNC-59 protein, C elegansunc-61 protein, C elegans

Identifiers

PMID17599066
PMCPMC1933406
OpenAlexW2106127933

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.