Evidence map›Paper›PMID 30420662›Full record

ArticleNature cell biology2018

Multiple phosphorylations control recruitment of the KMN network onto kinetochores.

Masatoshi Hara, Mariko Ariyoshi, Ei-Ichi Okumura, Tetsuya Hori, Tatsuo Fukagawa

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Nature cell biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
6.4field-weighted citation impact, top 2% 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

52 citing papers in PubMed, 96 citations in OpenAlex.

  1. Article
  2. Structure and function of the outer kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
  3. Dual Roads of CENP-A for Centromere Identification.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Binding site maturation modulated by molecular density underlies Ndc80 binding to kinetochore receptor CENP-T.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Structure of the human outer kinetochore KMN network complex.Nature structural & molecular biology · 2024
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Cell cycle control of kinetochore assembly.Nucleus (Austin, Tex.) · 2022
    Review
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 1 country.

Masatoshi HaraGraduate School of Frontier Biosciences, Osaka University, Osaka, Japan.
Mariko AriyoshiGraduate School of Frontier Biosciences, Osaka University, Osaka, Japan.
Ei-Ichi OkumuraLaboratory of Cell and Developmental Biology, Graduate School of Bioscience, Tokyo Institute of Technology, Yokohama, Japan.
Tetsuya HoriGraduate School of Frontier Biosciences, Osaka University, Osaka, Japan.
Tatsuo FukagawaGraduate School of Frontier Biosciences, Osaka University, Osaka, Japan. tfukagawa@fbs.osaka-u.ac.jp.ORCID http://orcid.org/0000-0001-8564-6852
Ube Frontier University · JPTokyo Institute of Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To establish a functional kinetochore, the constitutive centromere-associated network (CCAN) forms a foundation on the centromere and recruits the KMN network, which directly binds to spindle microtubules. The CENP-C and CENP-T pathways in the CCAN recruit the KMN network to kinetochores, independently. The CENP-C pathway has been considered the major scaffold for the KMN network in vertebrate CCAN. However, we demonstrate that it is mainly the CENP-T pathway that recruits the KMN network onto the kinetochores and that CENP-T-KMN interactions are essential in chicken DT40 cells. By contrast, less Ndc80 binds to the CENP-C pathway in mitosis and the Mis12-CENP-C association is decreased during mitotic progression, which is consistent with the finding that the Mis12 complex-CENP-C binding is dispensable for cell viability. Furthermore, we find that multiple phosphoregulations of CENP-T and the Mis12 complex make the CENP-T pathway dominant. These results provide key insights into kinetochore dynamics during mitotic progression.

Indexed as

Signal TransductionAnimalsCell Line, TumorCentromereChickensChromosomal Proteins, Non-HistoneKinetochoresMicrotubule-Associated ProteinsMicrotubulesMitosisMultiprotein ComplexesPhosphorylationProtein BindingSpindle Apparatuscentromere protein CChromosomal Proteins, Non-HistoneMicrotubule-Associated ProteinsMultiprotein Complexes

Identifiers

PMID30420662
OpenAlexW2900053775

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.