Evidence map›Paper›PMID 28410370›Full record

ArticlePLoS genetics2017

A systematic screen for morphological abnormalities during fission yeast sexual reproduction identifies a mechanism of actin aster formation for cell fusion.

Omaya Dudin, Laura Merlini, Felipe O Bendezú, Raphaël Groux, Vincent Vincenzetti, Sophie G Martin

Abstract read
In one paragraph

Article in PLoS genetics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Effects ofExperimental and therapeutic medicine · 2026
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  7. Effects ofCurrent issues in molecular biology · 2024
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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

6 authors.

Omaya DudinDepartment of Fundamental Microbiology, University of Lausanne, Lausanne, Switzerland.ORCID 0000-0002-6673-3149
Laura MerliniDepartment of Fundamental Microbiology, University of Lausanne, Lausanne, Switzerland.
Felipe O BendezúDepartment of Fundamental Microbiology, University of Lausanne, Lausanne, Switzerland.ORCID 0000-0003-4324-2993
Raphaël GrouxDepartment of Fundamental Microbiology, University of Lausanne, Lausanne, Switzerland.
Vincent VincenzettiDepartment of Fundamental Microbiology, University of Lausanne, Lausanne, Switzerland.
Sophie G MartinDepartment of Fundamental Microbiology, University of Lausanne, Lausanne, Switzerland.ORCID 0000-0002-5317-2557

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In non-motile fungi, sexual reproduction relies on strong morphogenetic changes in response to pheromone signaling. We report here on a systematic screen for morphological abnormalities of the mating process in fission yeast Schizosaccharomyces pombe. We derived a homothallic (self-fertile) collection of viable deletions, which, upon visual screening, revealed a plethora of phenotypes affecting all stages of the mating process, including cell polarization, cell fusion and sporulation. Cell fusion relies on the formation of the fusion focus, an aster-like F-actin structure that is marked by strong local accumulation of the myosin V Myo52, which concentrates secretion at the fusion site. A secondary screen for fusion-defective mutants identified the myosin V Myo51-associated coiled-coil proteins Rng8 and Rng9 as critical for the coalescence of the fusion focus. Indeed, rng8Δ and rng9Δ mutant cells exhibit multiple stable dots at the cell-cell contact site, instead of the single focus observed in wildtype. Rng8 and Rng9 accumulate on the fusion focus, dependent on Myo51 and tropomyosin Cdc8. A tropomyosin mutant allele, which compromises Rng8/9 localization but not actin binding, similarly leads to multiple stable dots instead of a single focus. By contrast, myo51 deletion does not strongly affect fusion focus coalescence. We propose that focusing of the actin filaments in the fusion aster primarily relies on Rng8/9-dependent cross-linking of tropomyosin-actin filaments.

Indexed as

Actin CytoskeletonActinsAmino Acid SequenceCell Cycle ProteinsCytoskeletonMyosinsMyosin Type VPhenotypeProtein BindingReproductionSchizosaccharomycesSchizosaccharomyces pombe ProteinsSequence DeletionActinsCdc8 protein, S pombeCell Cycle ProteinsMyo51 protein, S pombeMyo52 protein, S pombeMyosinsMyosin Type VRng8 protein, S pombeRng9 protein, S pombeSchizosaccharomyces pombe Proteins

Identifiers

PMID28410370
PMCPMC5409535

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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.