Evidence map›Paper›PMID 19923271›Full record

ArticleJournal of cell science2009

Ipl1-dependent phosphorylation of Dam1 is reduced by tension applied on kinetochores.

Patrick Keating, Najma Rachidi, Tomoyuki U Tanaka, Michael J R Stark

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.

0numbers the graph read from it
0cells of the map it votes in
50citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

50 citing papers in PubMed, 68 citations in OpenAlex.

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  16. Yeast Sphingolipid Phospholipase GeneMolecular and cellular biology · 2020
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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 2 institutions in 1 country.

Patrick KeatingWellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, MSI/WTB Complex, University of Dundee, Dundee, DD1 5EH, UK.
Najma Rachidi
Tomoyuki U Tanaka
Michael J R Stark
University of Dundee · GBWellcome Trust · GB

Funding

Biotechnology and Biological Sciences Research Council BB/F009453/1Medical Research Council G0701147Wellcome Trust 067210Wellcome Trust 083524
6 · The paper itself

Abstract

The conserved Aurora B protein kinase (Ipl1 in Saccharomyces cerevisiae) is essential for ensuring that sister kinetochores become attached to microtubules from opposite spindle poles (bi-orientation) before anaphase onset. When sister chromatids become attached to microtubules from a single pole, Aurora B/Ipl1 facilitates turnover of kinetochore-microtubule attachments. This process requires phosphorylation by Aurora B/Ipl1 of kinetochore components such as Dam1 in yeast. Once bi-orientation is established and tension is applied on kinetochores, Aurora B/Ipl1 must stop promoting this turnover, otherwise correct attachment would never be stabilised. How this is achieved remains elusive: it might be due to dephosphorylation of Aurora B/Ipl1 substrates at kinetochores, or might take place independently, for example because of conformational changes in kinetochores. Here, we show that Ipl1-dependent phosphorylation at crucial sites on Dam1 is maximal during S phase and minimal during metaphase, matching the cell cycle window when chromosome bi-orientation occurs. Intriguingly, when we reduced tension at kinetochores through failure to establish sister chromatid cohesion, Dam1 phosphorylation persisted in metaphase-arrested cells. We propose that Aurora B/Ipl1-facilitated bi-orientation is stabilised in response to tension at kinetochores by dephosphorylation of Dam1, resulting in termination of kinetochore-microtubule attachment turnover.

Indexed as

Aurora KinasesBlotting, WesternCell Cycle ProteinsIntracellular Signaling Peptides and ProteinsKinetochoresMicrotubule-Associated ProteinsMicrotubulesPhosphorylationProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAurora KinasesCell Cycle ProteinsDAM1 protein, S cerevisiaeIntracellular Signaling Peptides and ProteinsIPL1 protein, S cerevisiaeMicrotubule-Associated ProteinsProtein Serine-Threonine KinasesSaccharomyces cerevisiae Proteins

Identifiers

PMID19923271
PMCPMC2779135
OpenAlexW2078200159

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.