Evidence map›Paper›PMID 21353555›Full record

ArticleCurrent biology : CB2011

CENP-C is a structural platform for kinetochore assembly.

Marcin R Przewloka, Zsolt Venkei, Victor M Bolanos-Garcia, Janusz Debski, Michal Dadlez, David M Glover

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Current biology : CB, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 187 papers.

0numbers the graph read from it
0cells of the map it votes in
187citing papers in PubMed
11.9field-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

187 citing papers in PubMed, 269 citations in OpenAlex.

  1. Structure and function of the outer kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Retention of a singlebioRxiv : the preprint server for biology · 2025
    Article
  11. Article
  12. Article
  13. Article
  14. Sustainable integrative cell biology: CENP-C is guilty by association.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    Article
  15. The dynamic centromere.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    Review
  16. The dynamics of centromere assembly and disassembly during quiescence.bioRxiv : the preprint server for biology · 2025
    Article
  17. Article
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Marcin R PrzewlokaDepartment of Genetics, University of Cambridge, Cambridge, UK. mrp50@cam.ac.uk
Zsolt Venkei
Victor M Bolanos-Garcia
Janusz Debski
Michal Dadlez
David M Glover
University of Cambridge · GBInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PL

Funding

Biotechnology and Biological Sciences Research CouncilCancer Research UK 11431Medical Research Council G1001696
6 · The paper itself

Abstract

Centromeres provide a region of chromatin upon which kinetochores are assembled in mitosis. Centromeric protein C (CENP-C) is a core component of this centromeric chromatin that, when depleted, prevents the proper formation of both centromeres and kinetochores. CENP-C localizes to centromeres throughout the cell cycle via its C-terminal part, whereas its N-terminal part appears necessary for recruitment of some but not all components of the Mis12 complex of the kinetochore. We now find that all kinetochore proteins belonging to the KMN (KNL1/Spc105, the Mis12 complex, and the Ndc80 complex) network bind to the N-terminal part of Drosophila CENP-C. Moreover, we show that the Mis12 complex component Nnf1 interacts directly with CENP-C in vitro. To test whether CENP-C's N-terminal part was sufficient to recruit KMN proteins, we targeted it to the centrosome by fusing it to a domain of Plk4 kinase. The Mis12 and Ndc80 complexes and Spc105 protein were then all recruited to centrosomes at the expense of centromeres, leading to mitotic abnormalities typical of cells with defective kinetochores. Thus, the N-terminal part of Drosophila CENP-C is sufficient to recruit core kinetochore components and acts as the principal linkage between centromere and kinetochore during mitosis.

Indexed as

AnimalsBlotting, WesternCell Cycle ProteinsChromosomal Proteins, Non-HistoneCloning, MolecularDNA PrimersDrosophilaFluorescent Antibody TechniqueImage Processing, Computer-AssistedKinetochoresMass SpectrometryMicrotubule-Associated ProteinsMitosisMultiprotein ComplexesCell Cycle Proteinscentromere protein CChromosomal Proteins, Non-HistoneDNA PrimersMicrotubule-Associated ProteinsMultiprotein Complexes

Identifiers

PMID21353555
OpenAlexW1967249732

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.