Evidence map›Paper›PMID 22660415›Full record

ArticleNature cell biology2012

MPS1/Mph1 phosphorylates the kinetochore protein KNL1/Spc7 to recruit SAC components.

Yuya Yamagishi, Ching-Hui Yang, Yuji Tanno, Yoshinori Watanabe

Abstract read
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In one paragraph

Article in Nature cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 216 papers.

0numbers the graph read from it
0cells of the map it votes in
216citing papers in PubMed
13.8field-weighted citation impact, top 1% 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

216 citing papers in PubMed, 366 citations in OpenAlex.

  1. Review
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  8. Oocyte Kinetochores at the Nexus of Meiotic Drive and Segregation Fidelity.Advances in experimental medicine and biology · 2026
    Review
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  15. Science advances · 2025
    Article
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156 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.

Yuya YamagishiLaboratory of Chromosome Dynamics, Institute of Molecular and Cellular Biosciences, University of Tokyo, Yayoi, Tokyo 113-0032, Japan.
Ching-Hui Yang
Yuji Tanno
Yoshinori Watanabe
The University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The genomic stability of all organisms depends on the precise partition of chromosomes to daughter cells. The spindle assembly checkpoint (SAC) senses unattached kinetochores and prevents premature entry to anaphase, thus ensuring that all chromosomes attach to opposite spindle poles (bi-orientation) during mitosis. MPS1 is an evolutionarily conserved protein kinase required for the SAC and chromosome bi-orientation. Yet, its primary cellular substrate has remained elusive. We show that fission yeast Mph1 (MPS1 homologue) phosphorylates the kinetochore protein Spc7 (KNL1/Blinkin homologue) at the MELT repeat sequences. This phosphorylation promotes the in vitro binding to the Bub1-Bub3 complex, which is required for kinetochore-based SAC activation (Mad1-Mad2-Mad3 localization) and chromosome alignment. Accordingly, a non-phosphorylatable spc7-12A mutation abolishes kinetochore targeting of Bub1-Bub3, whereas a phospho-mimetic spc7-12E mutation forces them to localize at kinetochores throughout the entire cell cycle, even in the absence of Mph1. Thus, MPS1/Mph1 kinase locating at the unattached kinetochores initially creates a mark, which is crucial for SAC activation and chromosome bi-orientation. This mechanism seems to be conserved in human cells.

Indexed as

Chromosome SegregationM Phase Cell Cycle CheckpointsCell Cycle ProteinsChromosomal Proteins, Non-HistoneKinetochoresMad2 ProteinsMutationNuclear ProteinsPhosphorylationProtein BindingProtein KinasesProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSchizosaccharomycesSchizosaccharomyces pombe ProteinsTime FactorsBub1 protein, S pombeBub3 protein, S pombeCell Cycle ProteinsChromosomal Proteins, Non-Histonemad1 protein, S pombeMad2 Proteinsmad2 protein, S pombemad3 protein, S pombeMph1 protein, S pombeNuclear ProteinsProtein KinasesProtein Serine-Threonine KinasesRecombinant Fusion ProteinsSchizosaccharomyces pombe ProteinsSpc7 protein, S pombe

Identifiers

PMID22660415
OpenAlexW2017956756

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.