Evidence map›Paper›PMID 25688133›Full record

ArticleThe Journal of cell biology2015

The F-BAR Cdc15 promotes contractile ring formation through the direct recruitment of the formin Cdc12.

Alaina H Willet, Nathan A McDonald, K Adam Bohnert, Michelle A Baird, John R Allen, Michael W Davidson, Kathleen L Gould

Open access · hybridAbstract read
In one paragraph

Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
4.1field-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

52 citing papers in PubMed, 65 citations in OpenAlex.

  1. Article
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  8. Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
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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.

Alaina H WilletDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
Nathan A McDonaldDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
K Adam BohnertDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232.
Michelle A BairdNational High Magnetic Field Laboratory and Department of Biological Science, The Florida State University, Tallahassee, FL 32306 National High Magnetic Field Laboratory and Department of Biological Science, The Florida State University, Tallahassee, FL 32306.
John R AllenNational High Magnetic Field Laboratory and Department of Biological Science, The Florida State University, Tallahassee, FL 32306 National High Magnetic Field Laboratory and Department of Biological Science, The Florida State University, Tallahassee, FL 32306.
Michael W DavidsonNational High Magnetic Field Laboratory and Department of Biological Science, The Florida State University, Tallahassee, FL 32306 National High Magnetic Field Laboratory and Department of Biological Science, The Florida State University, Tallahassee, FL 32306.
Kathleen L GouldDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232 kathy.gould@vanderbilt.edu.
Vanderbilt University · USNational High Magnetic Field Laboratory · US

Funding

Integrated Biological Systems Training in OncologyT32CA119925 · NCI · VANDERBILT UNIVERSITY · PI Vivian Gama, William Patrick Tansey · 2008 to 2026
$7.6M
Regulation of CytokinesisR01GM101035 · NIGMS · VANDERBILT UNIVERSITY · PI GOULD, KATHLEEN L · 2012 to 2018
$2.8M
NCI NIH HHS T32 CA119925NCI NIH HHS T32-CA119925NIGMS NIH HHS GM101035NIGMS NIH HHS R01 GM101035
6 · The paper itself

Abstract

In Schizosaccharomyces pombe, cytokinesis requires the assembly and constriction of an actomyosin-based contractile ring (CR). Nucleation of F-actin for the CR requires a single formin, Cdc12, that localizes to the cell middle at mitotic onset. Although genetic requirements for formin Cdc12 recruitment have been determined, the molecular mechanisms dictating its targeting to the medial cortex during cytokinesis are unknown. In this paper, we define a short motif within the N terminus of Cdc12 that binds directly to the F-BAR domain of the scaffolding protein Cdc15. Mutations preventing the Cdc12-Cdc15 interaction resulted in reduced Cdc12, F-actin, and actin-binding proteins at the CR, which in turn led to a delay in CR formation and sensitivity to other perturbations of CR assembly. We conclude that Cdc15 contributes to CR formation and cytokinesis via formin Cdc12 recruitment, defining a novel cytokinetic function for an F-BAR domain.

Indexed as

Actin CytoskeletonActinsAmino Acid MotifsAmino Acid SequenceCell Cycle ProteinsContractile ProteinsCytokinesisCytoskeletal ProteinsGTPase-Activating ProteinsGTP-Binding ProteinsMutationMyosin Type IIProtein BindingProtein Structure, TertiarySchizosaccharomycesSchizosaccharomyces pombe ProteinsActinsCdc12 protein, S pombeCDC15 proteinCell Cycle ProteinsContractile ProteinsCytoskeletal ProteinsGTPase-Activating ProteinsGTP-Binding ProteinsMyosin Type IIRng2 protein, S pombeSchizosaccharomyces pombe Proteins

Identifiers

PMID25688133
PMCPMC4332253
OpenAlexW2076784079

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.