Evidence map›Paper›PMID 41261855›Full record

ArticleNucleic acids research2025

Nuclear DAB2IP regulates DNA replication initiation through activating PLK1-mediated HBO1 phosphorylation.

Zeng-Fu Shang, Lan Yu, Ciara Newman, Wei-Min Chen, Grant W Birdsong, Brett C Sharp, Michael D Story, Debabrata Saha, Anthony J Davis

Abstract read
In one paragraph

Article in Nucleic acids research, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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

9 authors.

Zeng-Fu ShangDepartment of Radiation Oncology, University of Texas Southwestern Medical Center, Dallas TX 75390, United States.ORCID 0000-0002-2396-1416
Lan YuDepartment of Pathology, University of Texas Southwestern Medical Center, Dallas TX 75390, United States.
Ciara NewmanDepartment of Radiation Oncology, University of Texas Southwestern Medical Center, Dallas TX 75390, United States.
Wei-Min ChenDepartment of Radiation Oncology, University of Texas Southwestern Medical Center, Dallas TX 75390, United States.ORCID 0000-0002-5247-7826
Grant W BirdsongDepartment of Radiation Oncology, University of Texas Southwestern Medical Center, Dallas TX 75390, United States.
Brett C SharpDepartment of Radiation Oncology, University of Texas Southwestern Medical Center, Dallas TX 75390, United States.
Michael D StoryDepartment of Radiation Oncology, University of Texas Southwestern Medical Center, Dallas TX 75390, United States.
Debabrata SahaDepartment of Radiation Oncology, University of Texas Southwestern Medical Center, Dallas TX 75390, United States.ORCID 0000-0003-3477-4111
Anthony J DavisDepartment of Radiation Oncology, University of Texas Southwestern Medical Center, Dallas TX 75390, United States.ORCID 0000-0003-0184-3651

Funding

National Institute of Health CA233594National Institute of Health CA276058NIH HHS CA175879
6 · The paper itself

Abstract

DAB2IP (Disabled homolog 2 interacting protein), a recognized tumor suppressor, plays a pivotal role in regulating various oncogenic pathways. Our previous research demonstrated that DAB2IP functions as a cell cycle regulator by facilitating PLK1-mediated mitosis progression. Here, we elucidate a novel function of DAB2IP in promoting DNA replication origin firing. Mechanistically, we identified that DAB2IP localizes to the nucleus, where it interacts with the histone acetyltransferase HBO1 and enhances the HBO1-PLK1 interaction. DAB2IP facilitates PLK1-mediated phosphorylation of HBO1, which subsequently promotes HBO1-directed acetylation of histone 3 at lysine 14 (H3K14Ac). This modification enables the loading of the minichromosome maintenance protein (MCM) complex onto chromatin, thereby supporting DNA replication and maintaining genome integrity. Additionally, we found that ATR regulates CDK1-mediated phosphorylation of DAB2IP, and that this phosphorylation is essential for the formation and activation of the HBO1-PLK1 complex. Ablation of DAB2IP phosphorylation results in increased genomic instability due to incomplete replication of genomic DNA, as evidenced by the accumulation of anaphase ultrafine bridges and 53BP1 nuclear bodies in G1 phase of the cell cycle. In summary, our findings underscore the critical regulatory role of DAB2IP in DNA replication initiation and genomic stability maintenance, providing new insights into its function in cellular homeostasis.

Indexed as

Cell Cycle ProteinsCell NucleusDNA ReplicationHistone AcetyltransferasesProtein Serine-Threonine KinasesProto-Oncogene Proteinsras GTPase-Activating ProteinsAcetylationAtaxia Telangiectasia Mutated ProteinsCDC2 Protein KinaseGenomic InstabilityHEK293 CellsHeLa CellsHistonesHumansPhosphorylationAtaxia Telangiectasia Mutated ProteinsATR protein, humanCDC2 Protein KinaseCell Cycle ProteinsHistone AcetyltransferasesHistonesKAT7 protein, humanPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene Proteinsras GTPase-Activating Proteins

Identifiers

PMID41261855
PMCPMC12630137

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.