Evidence map›Paper›PMID 29601579›Full record

ArticlePLoS genetics2018

Cell polarity protein Spa2 coordinates Chs2 incorporation at the division site in budding yeast.

Magdalena Foltman, Yasmina Filali-Mouncef, Damaso Crespo, Alberto Sanchez-Diaz

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.6field-weighted citation impact, top 35% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  5. Article
  6. Chitin Synthesis in Yeast: A Matter of Trafficking.International journal of molecular sciences · 2022
    Review
  7. Article
  8. Article
  9. The Role of the Cell Integrity Pathway in Septum Assembly in Yeast.Journal of fungi (Basel, Switzerland) · 2021
    Review
  10. Review
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

4 authors at 1 institution in 1 country.

Magdalena FoltmanInstituto de Biomedicina y Biotecnología de Cantabria, Universidad de Cantabria, CSIC, Santander, Spain.
Yasmina Filali-MouncefInstituto de Biomedicina y Biotecnología de Cantabria, Universidad de Cantabria, CSIC, Santander, Spain.ORCID 0000-0001-5081-3518
Damaso CrespoDepartamento de Anatomía y Biología Celular, Facultad de Medicina, Universidad de Cantabria, Santander, Spain.
Alberto Sanchez-DiazInstituto de Biomedicina y Biotecnología de Cantabria, Universidad de Cantabria, CSIC, Santander, Spain.ORCID 0000-0002-3308-4824
Universidad de Cantabria · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Deposition of additional plasma membrane and cargoes during cytokinesis in eukaryotic cells must be coordinated with actomyosin ring contraction, plasma membrane ingression and extracellular matrix remodelling. The process by which the secretory pathway promotes specific incorporation of key factors into the cytokinetic machinery is poorly understood. Here, we show that cell polarity protein Spa2 interacts with actomyosin ring components during cytokinesis. Spa2 directly binds to cytokinetic factors Cyk3 and Hof1. The lethal effects of deleting the SPA2 gene in the absence of either Cyk3 or Hof1 can be suppressed by expression of the hypermorphic allele of the essential chitin synthase II (Chs2), a transmembrane protein transported on secretory vesicles that makes the primary septum during cytokinesis. Spa2 also interacts directly with the chitin synthase Chs2. Interestingly, artificial incorporation of Chs2 into the cytokinetic machinery allows the localisation of Spa2 at the site of division. In addition, increased Spa2 protein levels promote Chs2 incorporation at the site of division and primary septum formation. Our data indicate that Spa2 is recruited to the cleavage site to co-operate with the secretory vesicle system and particular actomyosin ring components to promote the incorporation of Chs2 into the so-called 'ingression progression complexes' during cytokinesis in budding yeast.

Indexed as

Cell PolarityCytokinesisChitin SynthaseCytoskeletal ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsChitin SynthaseChs2 protein, S cerevisiaeCytoskeletal ProteinsSaccharomyces cerevisiae ProteinsSPA2 protein, S cerevisiae

Identifiers

PMID29601579
PMCPMC5895073
OpenAlexW2794602932

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.