Evidence map›Paper›PMID 22187426›Full record

ArticleThe Journal of biological chemistry2012

Characterization of spindle checkpoint kinase Mps1 reveals domain with functional and structural similarities to tetratricopeptide repeat motifs of Bub1 and BubR1 checkpoint kinases.

Semin Lee, Philippe Thebault, Luca Freschi, Sylvie Beaufils, Tom L Blundell, Christian R Landry, Victor M Bolanos-Garcia, Sabine Elowe

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 35 citations in OpenAlex.

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  10. Modular elements of the TPR domain in the Mps1 N terminus differentially target Mps1 to the centrosome and kinetochore.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  11. Article
  12. Dynamic localization of Mps1 kinase to kinetochores is essential for accurate spindle microtubule attachment.Proceedings of the National Academy of Sciences of the United States of America · 2015
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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

8 authors at 6 institutions in 4 countries.

Semin LeeDepartment of Biochemistry, University of Cambridge, 80 Tennis Court Road, Cambridge CB2 1GA, United Kingdom.
Philippe Thebault
Luca Freschi
Sylvie Beaufils
Tom L Blundell
Christian R Landry
Victor M Bolanos-Garcia
Sabine Elowe
Czech Academy of Sciences, Biology Centre · CZUniversité Laval · CACentre hospitalier universitaire de Québec · CACentre National de la Recherche Scientifique · FRInstitut de Physique de Rennes · FRUniversity of Cambridge · GB

Funding

Canadian Institutes of Health Research GMX-191597Wellcome Trust RG44650
6 · The paper itself

Abstract

Kinetochore targeting of the mitotic kinases Bub1, BubR1, and Mps1 has been implicated in efficient execution of their functions in the spindle checkpoint, the self-monitoring system of the eukaryotic cell cycle that ensures chromosome segregation occurs with high fidelity. In all three kinases, kinetochore docking is mediated by the N-terminal region of the protein. Deletions within this region result in checkpoint failure and chromosome segregation defects. Here, we use an interdisciplinary approach that includes biophysical, biochemical, cell biological, and bioinformatics methods to study the N-terminal region of human Mps1. We report the identification of a tandem repeat of the tetratricopeptide repeat (TPR) motif in the N-terminal kinetochore binding region of Mps1, with close homology to the tandem TPR motif of Bub1 and BubR1. Phylogenetic analysis indicates that TPR Mps1 was acquired after the split between deutorostomes and protostomes, as it is distinguishable in chordates and echinoderms. Overexpression of TPR Mps1 resulted in decreased efficiency of both chromosome alignment and mitotic arrest, likely through displacement of endogenous Mps1 from the kinetochore and decreased Mps1 catalytic activity. Taken together, our multidisciplinary strategy provides new insights into the evolution, structural organization, and function of Mps1 N-terminal region.

Indexed as

Computational BiologyM Phase Cell Cycle CheckpointsAmino Acid MotifsAnimalsCattleCell Cycle ProteinsChromosomes, HumanEnzyme StabilityEvolution, MolecularHeLa CellsHumansHydrogen-Ion ConcentrationMiceModels, MolecularProtein MultimerizationProtein Serine-Threonine KinasesBub1b protein, mouseBUB1 protein, humanBub1 protein, mouseBub1 spindle checkpoint proteinCell Cycle ProteinsProtein Serine-Threonine KinasesProtein-Tyrosine KinasesTTK protein, human

Identifiers

PMID22187426
PMCPMC3285366
OpenAlexW2091556818

What OpenQuestion holds

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LicenceCC BY-NC
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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.