Evidence map›Paper›PMID 26702831›Full record

ArticleDevelopmental cell2015

Oligomerization but Not Membrane Bending Underlies the Function of Certain F-BAR Proteins in Cell Motility and Cytokinesis.

Nathan A McDonald, Craig W Vander Kooi, Melanie D Ohi, Kathleen L Gould

Abstract read
In one paragraph

Article in Developmental cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing 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

56 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Fission yeast Pdk1 kinase regulates cytokinesis and eisosomes.bioRxiv : the preprint server for biology · 2025
    Article
  7. Article
  8. Characterization and comparison ofmicroPublication biology · 2025
    Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Nathan A McDonaldDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
Craig W Vander KooiDepartment of Molecular and Cellular Biochemistry, University of Kentucky, Lexington, KY 40535, USA.
Melanie D OhiDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
Kathleen L GouldDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA. Electronic address: kathy.gould@vanderbilt.edu.

Funding

Regulation of CytokinesisR01GM101035 · NIGMS · VANDERBILT UNIVERSITY · PI GOULD, KATHLEEN L · 2012 to 2018
$2.8M
NIGMS NIH HHS GM101035NIGMS NIH HHS R01 GM101035
6 · The paper itself

Abstract

F-BAR proteins function in diverse cellular processes by linking membranes to the actin cytoskeleton. Through oligomerization, multiple F-BAR domains can bend membranes into tubules, though the physiological importance of F-BAR-to-F-BAR assemblies is not yet known. Here, we investigate the F-BAR domain of the essential cytokinetic scaffold, Schizosaccharomyces pombe Cdc15, during cytokinesis. Challenging a widely held view that membrane deformation is a fundamental property of F-BARs, we report that the Cdc15 F-BAR binds, but does not deform, membranes in vivo or in vitro, and six human F-BAR domains-including those from Fer and RhoGAP4-share this property. Nevertheless, tip-to-tip interactions between F-BAR dimers are critical for Cdc15 oligomerization and high-avidity membrane binding, stabilization of contractile ring components at the medial cortex, and the fidelity of cytokinesis. F-BAR oligomerization is also critical for Fer and RhoGAP4 physiological function, demonstrating its broad importance to F-BAR proteins that function without membrane bending.

Indexed as

Protein MultimerizationActin CytoskeletonCarrier ProteinsCell Cycle ProteinsCell MembraneCytokinesisCytoskeletal ProteinsHumansSchizosaccharomycesSchizosaccharomyces pombe ProteinsCarrier ProteinsCell Cycle ProteinsCytoskeletal ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID26702831
PMCPMC4691284

What OpenQuestion holds

Textmetadata
LicenceTDM
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.