Evidence map›Paper›PMID 29051266›Full record

ArticleThe Journal of cell biology2017

SUMOylation of human septins is critical for septin filament bundling and cytokinesis.

David Ribet, Serena Boscaini, Clothilde Cauvin, Martin Siguier, Serge Mostowy, Arnaud Echard, Pascale Cossart

Abstract read
In one paragraph

Article in The Journal of cell biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

36 citing papers in PubMed.

  1. Article
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  5. Article
  6. Chemical Proteomics Reveals NMolecular & cellular proteomics : MCP · 2024
    Article
  7. The Roles of Septins in Regulating Fission Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  8. Article
  9. Article
  10. 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
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. The Structural Biology of Septins and Their Filaments: An Update.Frontiers in cell and developmental biology · 2021
    Review
  20. Septin Remodeling During Mammalian Cytokinesis.Frontiers in cell and developmental biology · 2021
    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.

David RibetUnité des Interactions Bactéries-Cellules, Institut Pasteur, Institut National de la Santé et de la Recherche Médicale, Institut National de la Recherche Agronomique, Paris, France.ORCID 0000-0003-1175-6471
Serena BoscainiUnité des Interactions Bactéries-Cellules, Institut Pasteur, Institut National de la Santé et de la Recherche Médicale, Institut National de la Recherche Agronomique, Paris, France.
Clothilde CauvinUnité de Trafic Membranaire et Division Cellulaire, Département de Biologie Cellulaire et Infection, Institut Pasteur, Paris, France.
Martin SiguierUnité des Interactions Bactéries-Cellules, Institut Pasteur, Institut National de la Santé et de la Recherche Médicale, Institut National de la Recherche Agronomique, Paris, France.
Serge MostowyMedical Research Council Centre for Molecular Bacteriology and Infection, Imperial College London, London, England, UK.
Arnaud EchardUnité de Trafic Membranaire et Division Cellulaire, Département de Biologie Cellulaire et Infection, Institut Pasteur, Paris, France arnaud.echard@pasteur.fr.
Pascale CossartUnité des Interactions Bactéries-Cellules, Institut Pasteur, Institut National de la Santé et de la Recherche Médicale, Institut National de la Recherche Agronomique, Paris, France pascale.cossart@pasteur.fr.ORCID 0000-0001-8871-6780

Funding

HSRD VA CDP 13-004Wellcome Trust
6 · The paper itself

Abstract

Septins are cytoskeletal proteins that assemble into nonpolar filaments. They are critical in diverse cellular functions, acting as scaffolds for protein recruitment and as diffusion barriers for subcellular compartmentalization. Human septins are encoded by 13 different genes and are classified into four groups based on sequence homology (SEPT2, SEPT3, SEPT6, and SEPT7 groups). In yeast, septins were among the first proteins reported to be modified by SUMOylation, a ubiquitin-like posttranslational modification. However, whether human septins could be modified by small ubiquitin-like modifiers (SUMOs) and what roles this modification may have in septin function remains unknown. In this study, we first show that septins from all four human septin groups can be covalently modified by SUMOs. We show in particular that endogenous SEPT7 is constitutively SUMOylated during the cell cycle. We then map SUMOylation sites to the C-terminal domain of septins belonging to the SEPT6 and SEPT7 groups and to the N-terminal domain of septins from the SEPT3 group. We finally demonstrate that expression of non-SUMOylatable septin variants from the SEPT6 and SEPT7 groups leads to aberrant septin bundle formation and defects in cytokinesis after furrow ingression. Altogether, our results demonstrate a pivotal role for SUMOylation in septin filament bundling and cell division.

Indexed as

Protein Processing, Post-TranslationalCell CompartmentationCell Cycle ProteinsCytokinesisCytoskeletonFluorescence Recovery After PhotobleachingGenes, ReporterGreen Fluorescent ProteinsHeLa CellsHumansMicroscopy, VideoOsteoblastsPhylogenySeptinsSumoylationCell Cycle ProteinsGreen Fluorescent ProteinsSEPTIN2 protein, humanseptin 3SEPTIN6 protein, humanSEPTIN7 protein, humanSeptins

Identifiers

PMID29051266
PMCPMC5716278

What OpenQuestion holds

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LicenceCC BY-NC-SA
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Registered trials

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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.