Evidence map›Paper›PMID 18430955›Full record

ArticleGenetics2008

The protease activity of yeast separase (esp1) is required for anaphase spindle elongation independently of its role in cleavage of cohesin.

Chris Baskerville, Marisa Segal, Steven I Reed

Open access · hybridAbstract read
In one paragraph

Article in Genetics, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.6field-weighted citation impact, top 19% 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

19 citing papers in PubMed, 35 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Mapping separase-mediated cleavage in situ.NAR genomics and bioinformatics · 2022
    Article
  5. Review
  6. PP2AJournal of cell science · 2020
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Chromosome segregation in plant meiosis.Frontiers in plant science · 2014
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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 2 institutions in 2 countries.

Chris BaskervilleDepartment of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
Marisa Segal
Steven I Reed
Scripps Research Institute · USUniversity of Cambridge · GB

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
–
Cancer Research UKNIGMS NIH HHS GM-38328NIGMS NIH HHS R01 GM038328NIGMS NIH HHS R37 GM038328
6 · The paper itself

Abstract

Separase is a caspase-family protease required for the metaphase-anaphase transition in eukaryotes. In budding yeast, the separase ortholog, Esp1, has been shown to cleave a subunit of cohesin, Mcd1 (Scc1), thereby releasing sister chromatids from cohesion and allowing anaphase. However, whether Esp1 has other substrates required for anaphase has been controversial. Whereas it has been reported that cleavage of Mcd1 is sufficient to trigger anaphase in the absence of Esp1 activation, another study using a temperature-sensitive esp1 mutant concluded that depletion of Mcd1 was not sufficient for anaphase in the absence of Esp1 function. Here we revisit the issue and demonstrate that neither depletion of Mcd1 nor ectopic cleavage of Mcd1 by Tev1 protease is sufficient to support anaphase in an esp1 temperature-sensitive mutant. Furthermore, we demonstrate that the catalytic activity of the Esp1 protease is required for this Mcd1-independent anaphase function. These data suggest that another protein, possibly a spindle-associated protein, is cleaved by Esp1 to allow anaphase. Such a function is consistent with the previous observation that Esp1 localizes to the mitotic spindle during anaphase.

Indexed as

AnaphaseAllelesAmino Acid SubstitutionCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsEndopeptidasesMutationNuclear ProteinsPeptidesPhosphoproteinsProtein Processing, Post-TranslationalSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSeparaseSister Chromatid ExchangeCell Cycle ProteinsChromosomal Proteins, Non-HistoneCohesinsEndopeptidasesESP1 protein, S cerevisiaeMCD1 protein, S cerevisiaeNuclear ProteinsPeptidesPhosphoproteinsSaccharomyces cerevisiae ProteinsSeparase

Identifiers

PMID18430955
PMCPMC2323821
OpenAlexW2102856928

What OpenQuestion holds

Textmetadata
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.