Evidence map›Paper›PMID 22891673›Full record

ArticleTraffic (Copenhagen, Denmark)2012

Fission yeast sec3 bridges the exocyst complex to the actin cytoskeleton.

Isabelle Jourdain, Hannah C Dooley, Takashi Toda

Open access · greenAbstract read
In one paragraph

Article in Traffic (Copenhagen, Denmark), 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.0field-weighted citation impact, top 28% 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

17 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Integrative structure and function of the yeast exocyst complex.Protein science : a publication of the Protein Society · 2020
    Article
  6. TwoThe Journal of cell biology · 2019
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. The Exocyst Complex in Health and Disease.Frontiers in cell and developmental biology · 2016
    Review
  14. Article
  15. Formins: linking cytoskeleton and endomembranes in plant cells.International journal of molecular sciences · 2014
    Review
  16. Review
  17. FAM190A deficiency creates a cell division defect.The American journal of pathology · 2013
    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

3 authors at 1 institution in 1 country.

Isabelle JourdainCell Regulation Laboratory, London Research Institute, Cancer Research UK, 44 Lincoln's Inn Fields, London, WC2A 3LY, UK. isabelle.jourdain@cancer.org.uk
Hannah C Dooley
Takashi Toda
The Honourable Society of Lincoln's Inn · GB

Funding

Cancer Research UK
6 · The paper itself

Abstract

The exocyst complex tethers post-Golgi secretory vesicles to the plasma membrane prior to docking and fusion. In this study, we identify Sec3, the missing component of the Schizosaccharomyces pombe exocyst complex (SpSec3). SpSec3 shares many properties with its orthologs, and its mutants are rescued by human Sec3/EXOC1. Although involved in exocytosis, SpSec3 does not appear to mark the site of exocyst complex assembly at the plasma membrane. It does, however, mark the sites of actin cytoskeleton recruitment and controls the organization of all three yeast actin structures: the actin cables, endocytic actin patches and actomyosin ring. Specifically, SpSec3 physically interacts with For3 and sec3 mutants have no actin cables as a result of a failure to polarize this nucleating formin. SpSec3 also interacts with actin patch components and sec3 mutants have depolarized actin patches of reduced endocytic capacity. Finally, the constriction and disassembly of the cytokinetic actomyosin ring is compromised in these sec3 mutant cells. We propose that a role of SpSec3 is to spatially couple actin machineries and their independently polarized regulators. As a consequence of its dual role in secretion and actin organization, Sec3 appears as a major co-ordinator of cell morphology in fission yeast.

Indexed as

Actin CytoskeletonActinsCell Cycle ProteinsCell MembraneExocytosisForminsMutationSchizosaccharomycesSchizosaccharomyces pombe ProteinsSecretory VesiclesVesicular Transport ProteinsActinsCell Cycle ProteinsFOR3 protein, S pombeForminsSchizosaccharomyces pombe ProteinsSec3 protein, S pombeVesicular Transport Proteins

Identifiers

PMID22891673
PMCPMC3531892
OpenAlexW1550284333

What OpenQuestion 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 OpenQuestion graph.