Evidence map›Paper›PMID 39979508›Full record

ArticleNature structural & molecular biology2025

Haspin kinase binds to a nucleosomal DNA supergroove.

Chad W Hicks, Colin R Gliech, Sanim Rahman, Xiangbin Zhang, Andrew S Eneim, Stacy J Vasquez, Andrew J Holland, Cynthia Wolberger

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2025. 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. Review
  2. Article
  3. Cryo-EM structure of ALC1 in an open conformation bound to a PARylated nucleosome.Acta crystallographica. Section D, Structural biology · 2026
    Article
  4. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors.

Chad W HicksDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Colin R GliechDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Sanim RahmanDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Xiangbin ZhangDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Andrew S EneimDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID http://orcid.org/0000-0002-3956-9654
Stacy J VasquezDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
Andrew J HollandDepartment of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD, USA.ORCID http://orcid.org/0000-0003-3728-6367
Cynthia WolbergerDepartment of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD, USA. cwolberg@jhmi.edu.ORCID http://orcid.org/0000-0001-8578-2969

Funding

Mechanistic studies of chromatin modification in transcription regulationR35GM130393 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Cynthia Wolberger · 2019 to 2026
$7.3M
Centrosome biogenesis and copy number controlR01GM114119 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI CORMACK, BRENDAN · 2015 to 2023
$3.3M
The role of TRIM37 in driving tumorigenesis and cancer-specific vulnerability to PLK4 inhibitionR01CA266199 · NCI · JOHNS HOPKINS UNIVERSITY · PI Sergi Regot · 2022 to 2026
$2.7M
Molecular mechanism that suppresses the proliferation of cells with supernumerary centriolesR01GM133897 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI CORMACK, BRENDAN · 2019 to 2022
$1.9M
Regulation and recognition of H3K79meF31CA261154 · NCI · JOHNS HOPKINS UNIVERSITY · PI HICKS, CHAD · 2021 to 2023
$139k
Molecular Basis of Histone Methylation by PRMT5F31CA271743 · NCI · JOHNS HOPKINS UNIVERSITY · PI RAHMAN, SANIM · 2023 to 2025
$117k
NCI NIH HHS F31 CA261154NCI NIH HHS F31 CA271743NCI NIH HHS R01 CA266199NIGMS NIH HHS R01 GM114119NIGMS NIH HHS R01 GM133897NIGMS NIH HHS R35 GM130393
6 · The paper itself

Abstract

Phosphorylation of histone H3 threonine 3 (H3T3) by Haspin recruits the chromosomal passenger complex to the inner centromere and ensures proper cell cycle progression through mitosis. The mechanism by which Haspin binds to nucleosomes to phosphorylate H3T3 is not known. Here we report cryogenic electron microscopy structures of the human Haspin kinase domain bound to a nucleosome. In contrast with previous structures of histone-modifying enzymes, Haspin solely contacts the nucleosomal DNA, inserting into a supergroove formed by apposing major grooves of two DNA gyres. This binding mode provides a plausible mechanism by which Haspin can bind to nucleosomes in a condensed chromatin environment to phosphorylate H3T3. We identify key basic residues in the Haspin kinase domain that are essential for phosphorylation of nucleosomal histone H3 and binding to mitotic chromatin. Our structural data provide notable insight into a histone-modifying enzyme that binds to nucleosomes solely through DNA contacts.

Indexed as

DNAIntracellular Signaling Peptides and ProteinsNucleosomesProtein Serine-Threonine KinasesCryoelectron MicroscopyHistonesHumansModels, MolecularPhosphorylationProtein BindingDNAHASPIN protein, humanHistonesIntracellular Signaling Peptides and ProteinsNucleosomesProtein Serine-Threonine Kinases

Identifiers

PMID39979508
PMCPMC12170164

What Socratic holds

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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 Socratic graph.