Evidence map›Paper›PMID 41629527›Full record

ArticleThe EMBO journal2026

M18BP1 valency and a distributed interaction footprint determine epigenetic centromere specification in humans.

Kai Walstein, Louisa Hill, Doro Vogt, Lina Oberste-Lehn, Petra Janning, Ingrid R Vetter, Dongqing Pan, Andrea Musacchio

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 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Dual Roads of CENP-A for Centromere Identification.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  2. Article
  3. Article
  4. Preserving centromere identity: right amounts of CENP-A at the right place and time.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2025
    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

8 authors.

Kai Walstein *Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany.ORCID http://orcid.org/0000-0002-2876-7903
Louisa Hill *Department of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany.ORCID http://orcid.org/0000-0002-6258-6161
Doro VogtDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany.ORCID http://orcid.org/0000-0002-3673-3711
Lina Oberste-LehnDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany.ORCID http://orcid.org/0009-0006-2977-4351
Petra JanningMass Spectrometry Facility, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany.
Ingrid R VetterDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany.ORCID http://orcid.org/0000-0002-1722-425X
Dongqing PanDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany.
Andrea MusacchioDepartment of Mechanistic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, Dortmund, 44227, Germany. andrea.musacchio@mpi-dortmund.mpg.de.ORCID http://orcid.org/0000-0003-2362-8784

Funding

Deutsche Forschungsgemeinschaft (DFG) Collaborative Research Centre 1430EC | Horizon Europe | Excellent Science | HORIZON EUROPE European Research Council (ERC) SyG 951430European Molecular Biology Organization (EMBO) ALFT106-2024
6 · The paper itself

Abstract

The histone H3 variant CENP-A is considered an epigenetic landmark of centromeres. Its deposition reflects cell-cycle-regulated assembly of M18BP1, HJURP, and PLK1 on a divalent MIS18α/β scaffold. The localization determinants of this machinery remain poorly characterized. Here, we report that in human cells, artificial M18BP1 dimerization bypasses MIS18α/β, allowing the identification of at least four determinants of M18BP1 centromere localization. These include the SANTA domain, of which we report the first structure, as well as linear motifs in disordered neighboring regions, of which we characterize the interaction footprint on the CENP-A-associated 16-subunit constitutive centromere-associated network (CCAN). Our observations imply that M18BP1, after dimerization, is necessary and sufficient for centromere localization. Its cell-cycle-dependent dimerization on MIS18α/β promotes initial recognition of a multivalent centromeric assembly of old CENP-A and associated proteins, followed by cooption of PLK1 and HJURP and new CENP-A deposition. Our results shed new light on the determinants of centromere epigenetic inheritance in humans.

Indexed as

CentromereEpigenesis, GeneticAdaptor Proteins, Signal TransducingCell CycleCell Cycle ProteinsCentromere Protein AChromosomal Proteins, Non-HistoneDNA-Binding ProteinsHeLa CellsHumansPolo-Like Kinase 1Protein BindingProtein MultimerizationProtein Serine-Threonine KinasesProto-Oncogene ProteinsAdaptor Proteins, Signal TransducingCell Cycle ProteinsCENPA protein, humanCentromere Protein AChromosomal Proteins, Non-HistoneDNA-Binding ProteinsHJURP protein, humanMIS18A protein, humanMIS18BP1 protein, humanPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsCell CycleCENP-A LoadingCentromereKinetochoreM18BP1

Identifiers

PMID41629527
PMCPMC12953894

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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.