Evidence map›Paper›PMID 22768263›Full record

ArticlePloS one2012

Fission yeast Sec3 and Exo70 are transported on actin cables and localize the exocyst complex to cell poles.

Felipe O Bendezú, Vincent Vincenzetti, Sophie G Martin

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

42 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Article
  3. Preassembly and independent trafficking of the exocyst complex inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. Review
  7. Emerging Roles of Exocyst Complex in Fungi: A Review.Journal of fungi (Basel, Switzerland) · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Integrative structure and function of the yeast exocyst complex.Protein science : a publication of the Protein Society · 2020
    Article
  18. Exocyst subunitJournal of biosciences · 2020
    Article
  19. International journal of molecular sciences · 2019
    Article
  20. 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.

Felipe O BendezúDepartment of Fundamental Microbiology, Faculty of Biology and Medicine, University of Lausanne, Lausanne, Switzerland.
Vincent Vincenzetti
Sophie G Martin
University of Lausanne · CH

Funding

European Research Council 260493
6 · The paper itself

Abstract

The exocyst complex is essential for many exocytic events, by tethering vesicles at the plasma membrane for fusion. In fission yeast, polarized exocytosis for growth relies on the combined action of the exocyst at cell poles and myosin-driven transport along actin cables. We report here the identification of fission yeast Schizosaccharomyces pombe Sec3 protein, which we identified through sequence homology of its PH-like domain. Like other exocyst subunits, sec3 is required for secretion and cell division. Cells deleted for sec3 are only conditionally lethal and can proliferate when osmotically stabilized. Sec3 is redundant with Exo70 for viability and for the localization of other exocyst subunits, suggesting these components act as exocyst tethers at the plasma membrane. Consistently, Sec3 localizes to zones of growth independently of other exocyst subunits but depends on PIP(2) and functional Cdc42. FRAP analysis shows that Sec3, like all other exocyst subunits, localizes to cell poles largely independently of the actin cytoskeleton. However, we show that Sec3, Exo70 and Sec5 are transported by the myosin V Myo52 along actin cables. These data suggest that the exocyst holocomplex, including Sec3 and Exo70, is present on exocytic vesicles, which can reach cell poles by either myosin-driven transport or random walk.

Indexed as

Cell PolarityActinsAmino Acid Sequencecdc42 GTP-Binding ProteinModels, BiologicalMolecular Sequence DataMultiprotein ComplexesMyosinsPhosphatidylinositol 4,5-DiphosphateProtein TransportSchizosaccharomycesSchizosaccharomyces pombe ProteinsVesicular Transport ProteinsActinscdc42 GTP-Binding ProteinEXO70 protein, S pombeMultiprotein ComplexesMyo52 protein, S pombeMyosinsPhosphatidylinositol 4,5-DiphosphateSchizosaccharomyces pombe ProteinsSec3 protein, S pombeVesicular Transport Proteins

Identifiers

PMID22768263
PMCPMC3386988
OpenAlexW2042261548

What OpenQuestion holds

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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.