Evidence map›Paper›PMID 35673994›Full record

ArticleJournal of cell science2022

Actin assembly requirements of the formin Fus1 to build the fusion focus.

Ingrid Billault-Chaumartin, Laetitia Michon, Caitlin A Anderson, Sarah E Yde, Cristian Suarez, Justyna Iwaszkiewicz, Vincent Zoete, David R Kovar, Sophie G Martin

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Journal of cell science, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.7field-weighted citation impact, top 36% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. 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

9 authors at 3 institutions in 2 countries.

Ingrid Billault-ChaumartinDepartment of Fundamental Microbiology, Faculty of Biology and Medicine, University of Lausanne, Biophore building, CH-1015 Lausanne, Switzerland.
Laetitia MichonDepartment of Fundamental Microbiology, Faculty of Biology and Medicine, University of Lausanne, Biophore building, CH-1015 Lausanne, Switzerland.
Caitlin A AndersonDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637, USA.
Sarah E YdeDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637, USA.
Cristian SuarezDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637, USA.ORCID 0000-0001-8279-3515
Justyna IwaszkiewiczMolecular Modeling Group, Swiss Institute of Bioinformatics, Amphipôle Building, CH-1015 Lausanne, Switzerland.
Vincent ZoeteMolecular Modeling Group, Swiss Institute of Bioinformatics, Amphipôle Building, CH-1015 Lausanne, Switzerland.
David R KovarDepartment of Molecular Genetics and Cell Biology, The University of Chicago, Chicago, IL 60637, USA.
Sophie G MartinDepartment of Fundamental Microbiology, Faculty of Biology and Medicine, University of Lausanne, Biophore building, CH-1015 Lausanne, Switzerland.ORCID 0000-0002-5317-2557
University of Chicago · USUniversity of Lausanne · CHSIB Swiss Institute of Bioinformatics · CH

Funding

Molecular And Cellular Biology Training ProgramT32GM007183 · NIGMS · UNIVERSITY OF CHICAGO · PI GLICK, BENJAMIN S, RICE, PHOEBE A · 1985 to 2021
$23.9M
Mechanisms of Formin-Mediated Actin Filament Assembly - Renewal 01 - ResubmissionR01GM079265 · NIGMS · UNIVERSITY OF CHICAGO · PI KOVAR, DAVID R · 2007 to 2023
$4.5M
European Research Council CoG CellFusionNIGMS NIH HHS R01 GM079265NIGMS NIH HHS T32 GM007183NIH HHS R01 GM079265NIH HHS T32 GM007183Schweizerischer Nationalfonds zur Forderung der Wissenschaftlichen Forschung 310030B_176396Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung 310030B_176396
6 · The paper itself

Abstract

In formin-family proteins, actin filament nucleation and elongation activities reside in the formin homology 1 (FH1) and FH2 domains, with reaction rates that vary by at least 20-fold between formins. Each cell expresses distinct formins that assemble one or several actin structures, raising the question of what confers each formin its specificity. Here, using the formin Fus1 in Schizosaccharomyces pombe, we systematically probed the importance of formin nucleation and elongation rates in vivo. Fus1 assembles the actin fusion focus, necessary for gamete fusion to form the zygote during sexual reproduction. By constructing chimeric formins with combinations of FH1 and FH2 domains previously characterized in vitro, we establish that changes in formin nucleation and elongation rates have direct consequences on fusion focus architecture, and that Fus1 native high nucleation and low elongation rates are optimal for fusion focus assembly. We further describe a point mutant in Fus1 FH2 that preserves native nucleation and elongation rates in vitro but alters function in vivo, indicating an additional FH2 domain property. Thus, rates of actin assembly are tailored for assembly of specific actin structures.

Indexed as

SchizosaccharomycesSchizosaccharomyces pombe ProteinsActin CytoskeletonActinsForminsMicrofilament ProteinsActinsForminsMicrofilament ProteinsSchizosaccharomyces pombe ProteinsActin cytoskeletonCell–cell fusionFission yeast Schizosaccharomyces pombeFormin

Identifiers

PMID35673994
PMCPMC9377709
OpenAlexW4282945618

What OpenQuestion holds

Textmetadata
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.