Evidence map›Paper›PMID 11149918›Full record

ArticleThe Journal of cell biology2001

A novel role of the budding yeast separin Esp1 in anaphase spindle elongation: evidence that proper spindle association of Esp1 is regulated by Pds1.

S Jensen, M Segal, D J Clarke, S I Reed

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

70 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Securin Regulates the Spatiotemporal Dynamics of Separase.bioRxiv : the preprint server for biology · 2023
    Article
  5. Review
  6. Accumulation of Securin on Spindle During Female Meiosis I.Frontiers in cell and developmental biology · 2021
    Article
  7. PP2AJournal of cell science · 2020
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

10 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

4 authors at 1 institution in 1 country.

S JensenDepartment of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
M Segal
D J Clarke
S I Reed
Scripps Research Institute · US

Funding

CONTROL OF CELL DIVISION IN YEASTR37GM038328 · NIGMS · SCRIPPS RESEARCH INSTITUTE, THE · PI REED, STEVEN I · 2000 to 2009
$4.3M
STUDIES ON THE CONTROL OF CELL DIVISION IN YEASTR01GM038328 · NIGMS · SCRIPPS RESEARCH INSTITUTE · PI REED, STEVEN I · 1987 to 1999
–
NIGMS NIH HHS GM38238NIGMS NIH HHS R01 GM038328NIGMS NIH HHS R37 GM038328
6 · The paper itself

Abstract

In Saccharomyces cerevisiae, the metaphase-anaphase transition is initiated by the anaphase-promoting complex-dependent degradation of Pds1, whereby Esp1 is activated to promote sister chromatid separation. Although this is a fundamental step in the cell cycle, little is known about the regulation of Esp1 and how loss of cohesion is coordinated with movement of the anaphase spindle. Here, we show that Esp1 has a novel role in promoting anaphase spindle elongation. The localization of Esp1 to the spindle apparatus, analyzed by live cell imaging, is regulated in a manner consistent with a function during anaphase B. The protein accumulates in the nucleus in G2 and is mobilized onto the spindle pole bodies and spindle midzone at anaphase onset, where it persists into midanaphase. Association with Pds1 occurs during S phase and is required for efficient nuclear targeting of Esp1. Spindle association is not fully restored in pds1 mutants expressing an Esp1-nuclear localization sequence fusion protein, suggesting that Pds1 is also required to promote Esp1 spindle binding. In agreement, Pds1 interacts with the spindle at the metaphase-anaphase transition and a fraction remains at the spindle pole bodies and the spindle midzone in anaphase cells. Finally, mutational analysis reveals that the conserved COOH-terminal region of Esp1 is important for spindle interaction.

Indexed as

EndopeptidasesSaccharomyces cerevisiae ProteinsAnaphaseBinding SitesBiological TransportCalciumCell CycleCell Cycle ProteinsCell NucleusFungal ProteinsNuclear ProteinsSaccharomyces cerevisiaeSecurinSeparaseSpindle ApparatusCalciumCell Cycle ProteinsEndopeptidasesESP1 protein, S cerevisiaeFungal ProteinsNuclear ProteinsPDS1 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSecurinSeparase

Identifiers

PMID11149918
PMCPMC2193664
OpenAlexW2137603270

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.