Evidence map›Paper›PMID 41507393›Full record

ArticleThe EMBO journal2026

Dual pathways via CENP-C and Mis18C recruit HJURP for CENP-A deposition into vertebrate centromeres.

Tetsuya Hori, Yutaka Mahana, Mariko Ariyoshi, Tatsuo Fukagawa

Abstract read
In one paragraph

Article in The EMBO journal, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Structure and function of the centromere and inner kinetochore.Nature reviews. Molecular cell biology · 2026
    Review
  2. Article
  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. The CENP-A chaperone complex spatially organizes centromeres.bioRxiv : the preprint server for biology · 2025
    Article
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.

Tetsuya HoriGraduate School of Frontier Biosciences, The University of Osaka, Suita, Osaka, 565-0871, Japan. t.hori.fbs@osaka-u.ac.jp.ORCID http://orcid.org/0000-0002-0363-4688
Yutaka MahanaGraduate School of Frontier Biosciences, The University of Osaka, Suita, Osaka, 565-0871, Japan.ORCID http://orcid.org/0000-0001-6218-6726
Mariko AriyoshiGraduate School of Frontier Biosciences, The University of Osaka, Suita, Osaka, 565-0871, Japan.ORCID http://orcid.org/0000-0002-1361-2642
Tatsuo FukagawaGraduate School of Frontier Biosciences, The University of Osaka, Suita, Osaka, 565-0871, Japan. fukagawa.tatsuo.fbs@osaka-u.ac.jp.ORCID http://orcid.org/0000-0001-8564-6852

Funding

MEXT | Japan Society for the Promotion of Science (JSPS) 22H00408MEXT | Japan Society for the Promotion of Science (JSPS) 23K18113MEXT | Japan Society for the Promotion of Science (JSPS) 23K27153MEXT | Japan Society for the Promotion of Science (JSPS) 24H02281MEXT | Japan Society for the Promotion of Science (JSPS) 24K09340MEXT | Japan Society for the Promotion of Science (JSPS) 24K23185MEXT | Japan Society for the Promotion of Science (JSPS) 25H00975MEXT | JST | Core Research for Evolutional Science and Technology of Japan Science and Technology Agency (CREST) JPMJCR21E6
6 · The paper itself

Abstract

Centromere position is specified and maintained by sequence-independent epigenetic mechanisms in vertebrate cells, with the incorporation of the centromere-specific histone H3 variant CENP-A into chromatin being a key event for centromere specification. Although many models for CENP-A incorporation have been proposed, much remains unknown. In this study, we reveal that the CENP-A chaperone HJURP directly binds to the C-terminal domain of chicken CENP-C in vitro and that this interaction is essential for new CENP-A incorporation in chicken DT40 cells. While existing models have suggested that HJURP is recruited by the Mis18 complex (Mis18C), here, we propose that CENP-C and Mis18C provide dual recruitment pathways for HJURP localization to centromeres in DT40 cells. We demonstrate that both HJURP localization and new CENP-A incorporation are completely abolished in Mis18C knockout cells expressing an HJURP mutant lacking CENP-C binding ability. Furthermore, co-immunoprecipitation experiments reveal that CENP-C, HJURP and Mis18C form a tight association in the chromatin fraction. These two pathways are critical for robust CENP-A incorporation to maintain centromere position in vertebrate cells.

Indexed as

AutoantigensCentromereChromosomal Proteins, Non-HistoneDNA-Binding ProteinsAnimalsCell LineCentromere Protein AChickensProtein BindingAutoantigensCentromere Protein Acentromere protein CChromosomal Proteins, Non-HistoneDNA-Binding ProteinsCENP-ACENP-CCentromereHJURPMis18 Complex

Identifiers

PMID41507393
PMCPMC12910082

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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.