Evidence map›Paper›PMID 22561346›Full record

ArticleNature cell biology2012

CENP-T proteins are conserved centromere receptors of the Ndc80 complex.

Alexander Schleiffer, Michael Maier, Gabriele Litos, Fabienne Lampert, Peter Hornung, Karl Mechtler, Stefan Westermann

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 125 papers.

0numbers the graph read from it
0cells of the map it votes in
125citing 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

125 citing papers in PubMed.

  1. Review
  2. Structure and function of the outer kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
  3. Structure and function of the centromere and inner kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
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  20. Cell cycle control of kinetochore assembly.Nucleus (Austin, Tex.) · 2022
    Review

65 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Alexander SchleifferIMP/IMBA Bioinformatics Core Facility, Research Institute of Molecular Pathology, Dr. Bohr Gasse 7, 1030 Vienna, Austria.
Michael Maier
Gabriele Litos
Fabienne Lampert
Peter Hornung
Karl Mechtler
Stefan Westermann

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Centromeres direct the assembly of kinetochores, microtubule-attachment sites that allow chromosome segregation on the mitotic spindle. Fundamental differences in size and organization between evolutionarily distant eukaryotic centromeres have in many cases obscured general principles of their function. Here we demonstrate that centromere-binding proteins are highly conserved between budding yeast and humans. We identify the histone-fold protein Cnn1(CENP-T) as a direct centromere receptor of the microtubule-binding Ndc80 complex. The amino terminus of Cnn1 contains a conserved peptide motif that mediates stoichiometric binding to the Spc24-25 domain of the Ndc80 complex. Consistent with the critical role of this interaction, artificial tethering of the Ndc80 complex through Cnn1 allows mini-chromosomes to segregate in the absence of a natural centromere. Our results reveal the molecular function of CENP-T proteins and demonstrate how the Ndc80 complex is anchored to centromeres in a manner that couples chromosome movement to spindle dynamics.

Indexed as

Amino Acid SequenceAnimalsCalcium-Binding ProteinsCalponinsCentromereChromosomal Proteins, Non-HistoneConserved SequenceCytoskeletal ProteinsEvolution, MolecularHumansMicrofilament ProteinsMolecular Sequence DataNuclear ProteinsProtein BindingSequence AlignmentCalcium-Binding ProteinsCalponinsCENPT protein, humanChromosomal Proteins, Non-HistoneCytoskeletal ProteinsMicrofilament ProteinsNDC80 protein, humanNuclear Proteins

Identifiers

PMID22561346

What OpenQuestion holds

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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.