Evidence map›Paper›PMID 11076964›Full record

ArticleThe Journal of cell biology2000

Fission yeast myosin-I, Myo1p, stimulates actin assembly by Arp2/3 complex and shares functions with WASp.

W L Lee, M Bezanilla, T D Pollard

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
4.9field-weighted citation impact, top 4% 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

80 citing papers in PubMed, 176 citations in OpenAlex.

  1. Article
  2. Regulation of Yeast Cytokinesis by Calcium.Journal of fungi (Basel, Switzerland) · 2025
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Unconventional Myosins fromBiomolecules · 2022
    Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. TheJournal of cell science · 2019
    Article
  18. Review
  19. Article
  20. Article

20 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

W L LeeGraduate Program in Biochemistry, Cellular and Molecular Biology, Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
M Bezanilla
T D Pollard
Salk Institute for Biological Studies · USJohns Hopkins University · US

Funding

Mechanism of cytokinesis in fission yeastR01GM026132 · NIGMS · YALE UNIVERSITY · PI POLLARD, THOMAS D. · 1985 to 2021
$8.8M
ACTIN-MYOSIN INTERACTIONS IN CELL MOTILITYR37GM026132 · NIGMS · SALK INSTITUTE FOR BIOLOGICAL STUDIES · PI POLLARD, THOMAS D. · 1988 to 1997
–
NIGMS NIH HHS GM-26132NIGMS NIH HHS R01 GM026132NIGMS NIH HHS R37 GM026132
6 · The paper itself

Abstract

Fission yeast myo1(+) encodes a myosin-I with all three tail homology domains (TH1, 2, 3) found in typical long-tailed myosin-Is. Myo1p tail also contains a COOH-terminal acidic region similar to the A-domain of WASp/Scar proteins and other fungal myosin-Is. Our analysis shows that Myo1p and Wsp1p, the fission yeast WASp-like protein, share functions and cooperate in controlling actin assembly. First, Myo1p localizes to cortical patches enriched at tips of growing cells and at sites of cell division. Myo1p patches partially colocalize with actin patches and are dependent on an intact actin cytoskeleton. Second, although deletion of myo1(+) is not lethal, Deltamyo1 cells have actin cytoskeletal defects, including loss of polarized cell growth, delocalized actin patches, and mating defects. Third, additional disruption of wsp1(+) is synthetically lethal, suggesting that these genes may share functions. In mapping the domains of Myo1p tail that share function with Wsp1p, we discovered that a Myo1p construct with just the head and TH1 domains is sufficient for cortical localization and to rescue all Deltamyo1 defects. However, it fails to rescue the Deltamyo1 Deltawsp1 lethality. Additional tail domains, TH2 and TH3, are required to complement the double mutant. Fourth, we show that a recombinant Myo1p tail binds to Arp2/3 complex and activates its actin nucleation activity.

Indexed as

Calmodulin-Binding ProteinsCytoskeletal ProteinsSchizosaccharomyces pombe ProteinsActin-Related Protein 2Actin-Related Protein 3ActinsAmino Acid SequenceAnimalsCell DivisionCloning, MolecularFungal ProteinsGenetic Complementation TestGenotypeHumansKineticsMolecular Sequence DataActin-Related Protein 2Actin-Related Protein 3ActinsACTR2 protein, humanACTR3 protein, humanCalmodulin-Binding ProteinsCytoskeletal ProteinsFungal ProteinsMYO1A protein, humanmyo1 protein, S pombeMyosin Heavy ChainsMyosin Type IRecombinant Fusion ProteinsRecombinant ProteinsSchizosaccharomyces pombe ProteinsWsp1 protein, S pombe

Identifiers

PMID11076964
PMCPMC2169449
OpenAlexW2004900153

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.