Evidence map›Paper›PMID 41956986›Full record

ArticleThe Journal of cell biology2026

Assembly and phosphoregulatory mechanisms of the budding yeast outer kinetochore KMN complex.

Noah N Turner, Ziguo Zhang, Jing Yang, Kyle W Muir, Stephen H McLaughlin, Tomos Morgan, David Barford

Abstract read
In one paragraph

Article in The Journal of cell biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Review
  2. Structure and function of the outer kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
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

7 authors.

Noah N TurnerMRC Laboratory of Molecular Biology , Cambridge, UK.ORCID 0009-0007-4802-9047
Ziguo ZhangMRC Laboratory of Molecular Biology , Cambridge, UK.ORCID 0000-0002-7268-9631
Jing YangMRC Laboratory of Molecular Biology , Cambridge, UK.ORCID 0000-0002-8984-4503
Kyle W MuirMRC Laboratory of Molecular Biology , Cambridge, UK.ORCID 0000-0002-0294-5679
Stephen H McLaughlinMRC Laboratory of Molecular Biology , Cambridge, UK.ORCID 0000-0001-9135-6253
Tomos MorganMRC Laboratory of Molecular Biology , Cambridge, UK.ORCID 0000-0002-3366-8889
David BarfordMRC Laboratory of Molecular Biology , Cambridge, UK.ORCID 0000-0001-8810-950X

Funding

Cancer Research UK C576/A14109Cancer Research UK C576/A25675Medical Research Council MC_UP_1201/6MRC Laboratory of Molecular Biology
6 · The paper itself

Abstract

During mitosis and meiosis, kinetochores mediate interactions between chromosomes and spindle microtubules. Kinetochores are multi-megadalton protein complexes essential for chromosome segregation; however, recent structural, functional, and evolutionary studies have revealed divergent mechanisms of kinetochore assembly. Here, we use cryo-EM to understand the structural mechanisms by which the budding yeast microtubule-binding outer kinetochore KMN complex assembles, and how its interactions with the centromere-binding inner kinetochore are regulated. The KMN complex comprises three subcomplexes: Knl1c, Mis12cMtw1c, and Ndc80c. We show how C-terminal motifs of the Mis12cMtw1c subunits Dsn1, Mis12Mtw1, and Nnf1 bind Knl1c and Ndc80c. At the opposite end of the Mis12cMtw1c stalk, an N-terminal auto-inhibitory segment of Dsn1 (Dsn1AI) folds into two α-helices that engage the Mis12cMtw1c head 1 domain, thereby occluding binding sites for the inner kinetochore subunits CENP-CMif2 and CENP-UAme1, reducing their affinity for Mis12cMtw1. Our structure reveals how Aurora BIpl1 phosphorylation of Dsn1AI would release this auto-inhibition to substantially strengthen preexisting connections between the inner and outer kinetochore.

Indexed as

KinetochoresMicrotubule-Associated ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsCryoelectron MicroscopyMicrotubulesNuclear ProteinsPhosphorylationProtein BindingMicrotubule-Associated ProteinsNDC80 protein, S cerevisiaeNuclear ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID41956986
PMCPMC13065467

What OpenQuestion holds

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Registered trials

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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.