Evidence map›Paper›PMID 26776521›Full record

ArticleCell reports2016

The Tubulation Activity of a Fission Yeast F-BAR Protein Is Dispensable for Its Function in Cytokinesis.

Nathan A McDonald, Yoshimasa Takizawa, Anna Feoktistova, Ping Xu, Melanie D Ohi, Craig W Vander Kooi, Kathleen L Gould

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

22 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
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  5. Review
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  9. Review
  10. Article
  11. Fission yeast Opy1 is an endogenous PI(4,5)PJournal of cell science · 2020
    Article
  12. Article
  13. Article
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  15. Article
  16. Review
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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 2 institutions in 1 country.

Nathan A McDonaldDepartment of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37240, USA.
Yoshimasa TakizawaDepartment of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37240, USA; Center for Structural Biology, Vanderbilt University, Nashville, TN 37240, USA.
Anna FeoktistovaDepartment of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37240, USA.
Ping XuDepartment of Molecular and Cellular Biochemistry and Center for Structural Biology, University of Kentucky, Lexington, KY 40536, USA.
Melanie D OhiDepartment of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37240, USA; Center for Structural Biology, Vanderbilt University, Nashville, TN 37240, USA.
Craig W Vander KooiDepartment of Molecular and Cellular Biochemistry and Center for Structural Biology, University of Kentucky, Lexington, KY 40536, USA.
Kathleen L GouldDepartment of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37240, USA. Electronic address: kathy.gould@vanderbilt.edu.
Vanderbilt University · USUniversity of Kentucky · US

Funding

Center for Biomedical Research Excellence in the Molecular Basis of Human DiseaseP20GM103486 · NIGMS · UNIVERSITY OF KENTUCKY · PI LOUIS HERSH, LOUIS HERSH LOUIS HERSH · 2012 to 2013
$4.2M
Regulation of CytokinesisR01GM101035 · NIGMS · VANDERBILT UNIVERSITY · PI GOULD, KATHLEEN L · 2012 to 2018
$2.8M
GPU-Accelerated Parallel Computer for Drug Discovery ApplicationsS10OD020154 · OD · VANDERBILT UNIVERSITY · PI SMITH, JARROD ANSON · 2015 to 2015
$225k
NIGMS NIH HHS GM101035NIGMS NIH HHS P20 GM103486NIGMS NIH HHS P20GM103486NIGMS NIH HHS R01 GM101035
6 · The paper itself

Abstract

F-BAR proteins link cellular membranes to the actin cytoskeleton in many biological processes. Here we investigated the function of the Schizosaccharomyces pombe Imp2 F-BAR domain in cytokinesis and find that it is critical for Imp2's role in contractile ring constriction and disassembly. To understand mechanistically how the F-BAR domain functions, we determined its structure, elucidated how it interacts with membranes, and identified an interaction between dimers that allows helical oligomerization and membrane tubulation. Using mutations that block either membrane binding or tubulation, we find that membrane binding is required for Imp2's cytokinetic function but that oligomerization and tubulation, activities often deemed central to F-BAR protein function, are dispensable. Accordingly, F-BARs that do not have the capacity to tubulate membranes functionally substitute for the Imp2 F-BAR, establishing that its major role is as a cell-cycle-regulated bridge between the membrane and Imp2 protein partners, rather than as a driver of membrane curvature.

Indexed as

AnimalsChlorocebus aethiopsCOS CellsCrystallography, X-RayCytokinesisCytoskeletal ProteinsDimerizationLiposomesMicroscopy, ElectronProtein Structure, TertiaryRecombinant ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsCytoskeletal ProteinsIMP2 protein, S pombeLiposomesRecombinant ProteinsSchizosaccharomyces pombe Proteins

Identifiers

PMID26776521
PMCPMC4731314
OpenAlexW2237980791

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.