Evidence map›Paper›PMID 23926047›Full record

ArticleOpen biology2013

Drosophila F-BAR protein Syndapin contributes to coupling the plasma membrane and contractile ring in cytokinesis.

Tetsuya Takeda, Iain M Robinson, Matthew M Savoian, John R Griffiths, Anthony D Whetton, Harvey T McMahon, David M Glover

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

20 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. PACSIN proteins in vivo: Roles in development and physiology.Acta physiologica (Oxford, England) · 2022
    Review
  7. Article
  8. Review
  9. Article
  10. Article
  11. IPIP27 Coordinates PtdIns(4,5)PCurrent biology : CB · 2019
    Article
  12. Review
  13. Cytokinesis in Metazoa and Fungi.Cold Spring Harbor perspectives in biology · 2017
    Review
  14. Article
  15. Coupling changes in cell shape to chromosome segregation.Nature reviews. Molecular cell biology · 2016
    Review
  16. Article
  17. Article
  18. Article
  19. Cytokinesis in animal cells.Cold Spring Harbor perspectives in biology · 2015
    Review
  20. Article
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 5 institutions in 1 country.

Tetsuya TakedaDepartment of Genetics, University of Cambridge, Downing Street, Cambridge CB2 3EH, UK. ttakeda@mrc-lmb.cam.ac.uk
Iain M Robinson
Matthew M Savoian
John R Griffiths
Anthony D Whetton
Harvey T McMahon
David M Glover
University of Cambridge · GBManchester Academic Health Science Centre · GBMRC Laboratory of Molecular Biology · GBPeninsula College of Medicine and Dentistry · GBUniversity of Manchester · GB

Funding

Cancer Research UK 11431Cancer Research UK C3/A11431Medical Research Council G0802208Medical Research Council MC_U105178795Medical Research Council U105178795
6 · The paper itself

Abstract

Cytokinesis is a highly ordered cellular process driven by interactions between central spindle microtubules and the actomyosin contractile ring linked to the dynamic remodelling of the plasma membrane. The mechanisms responsible for reorganizing the plasma membrane at the cell equator and its coupling to the contractile ring in cytokinesis are poorly understood. We report here that Syndapin, a protein containing an F-BAR domain required for membrane curvature, contributes to the remodelling of the plasma membrane around the contractile ring for cytokinesis. Syndapin colocalizes with phosphatidylinositol 4,5-bisphosphate (PI(4,5)P₂) at the cleavage furrow, where it directly interacts with a contractile ring component, Anillin. Accordingly, Anillin is mislocalized during cytokinesis in Syndapin mutants. Elevated or diminished expression of Syndapin leads to cytokinesis defects with abnormal cortical dynamics. The minimal segment of Syndapin, which is able to localize to the cleavage furrow and induce cytokinesis defects, is the F-BAR domain and its immediate C-terminal sequences. Phosphorylation of this region prevents this functional interaction, resulting in reduced ability of Syndapin to bind to and deform membranes. Thus, the dephosphorylated form of Syndapin mediates both remodelling of the plasma membrane and its proper coupling to the cytokinetic machinery.

Indexed as

Actin CytoskeletonAnimalsCarrier ProteinsCell LineCell MembraneContractile ProteinsCytokinesisDrosophila melanogasterDrosophila ProteinsMicrofilament ProteinsMicrotubulesPhosphatidylinositol 4,5-DiphosphateProtein Processing, Post-TranslationalanillinCarrier ProteinsContractile ProteinsDrosophila ProteinsMicrofilament ProteinsPhosphatidylinositol 4,5-DiphosphateSynd protein, Drosophilaactomyosin contractile ringcytokinesisF-BARmembranephosphorylation

Identifiers

PMID23926047
PMCPMC3758542
OpenAlexW2140924653

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.