Evidence map›Paper›PMID 25609707›Full record

ArticleJournal of cell science2015

Subnuclear domain proteins in cancer cells support the functions of RUNX2 in the DNA damage response.

Seungchan Yang, Alexandre J C Quaresma, Jeffrey A Nickerson, Karin M Green, Scott A Shaffer, Anthony N Imbalzano, Lori A Martin-Buley, Jane B Lian, Janet L Stein, Andre J van Wijnen and 1 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

16 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
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  4. Review
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  8. The emerging role of ISWI chromatin remodeling complexes in cancer.Journal of experimental & clinical cancer research : CR · 2021
    Review
  9. Article
  10. Article
  11. Article
  12. Hypoxia-related microRNA-210 is a diagnostic marker for discriminating osteoblastoma and osteosarcoma.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2017
    Article
  13. Review
  14. Article
  15. Article
  16. 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

11 authors at 4 institutions in 2 countries.

Seungchan YangDepartment of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA.
Alexandre J C QuaresmaDepartment of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA Institute of Biomedicine, Department of Biochemistry and Developmental Biology, FI-00014 University of Helsinki, Finland.
Jeffrey A NickersonDepartment of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA.
Karin M GreenDepartment of Biochemistry and Molecular Pharmacology and Proteomics and Mass Spectrometry Facility, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Scott A ShafferDepartment of Biochemistry and Molecular Pharmacology and Proteomics and Mass Spectrometry Facility, University of Massachusetts Medical School, Worcester, MA 01605, USA.
Anthony N ImbalzanoDepartment of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA.
Lori A Martin-BuleyDepartment of Biochemistry & Vermont Cancer Center, University of Vermont Medical School, Burlington, VT 05405, USA.
Jane B LianDepartment of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA Department of Biochemistry & Vermont Cancer Center, University of Vermont Medical School, Burlington, VT 05405, USA.
Janet L SteinDepartment of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA Department of Biochemistry & Vermont Cancer Center, University of Vermont Medical School, Burlington, VT 05405, USA.
Andre J van WijnenDepartment of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA Departments of Orthopedic Surgery & Biochemistry and Molecular Biology, Mayo Clinic, 200 First Street S.W., MSB 3-69, Rochester, MN 55905, USA.
Gary S SteinDepartment of Cell Biology, University of Massachusetts Medical School, Worcester, MA 01655, USA Department of Biochemistry & Vermont Cancer Center, University of Vermont Medical School, Burlington, VT 05405, USA gary.stein@uvm.edu.
University of Massachusetts Chan Medical School · USUniversity of Vermont · USUniversity of Helsinki · FIUniversity of Vermont Medical Center · US

Funding

SUBNUCLEAR TARGETING OF TRANSCRIPTION FACTORSP01CA082834 · NCI · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STEIN, GARY S. · 2001 to 2015
$18.4M
Subnuclear Integration of Regulatory Signals Controlling Bone Cell FunctionP01AR048818 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI STEIN, JANET L · 2002 to 2011
$14.0M
CONTROL OF OSTEOBLAST PROLIFERATION AND DIFFERENTIATIONR01AR039588 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LIAN, JANE B., STEIN, GARY S. · 1990 to 2019
$8.0M
Molecular Control of Bone FormationR01AR049069 · NIAMS · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI WESTENDORF, JENNIFER J · 2003 to 2021
$5.8M
Synthesis of Osteocalcin in BoneR37DE012528 · NIDCR · UNIV OF MASSACHUSETTS MED SCH WORCESTER · PI LIAN, JANE B. · 2008 to 2017
$5.0M
NCI NIH HHS P01 CA082834NIAMS NIH HHS P01 AR048818NIAMS NIH HHS R01 AR039588NIAMS NIH HHS R01 AR049069NIDCR NIH HHS R37 DE012528
6 · The paper itself

Abstract

Cancer cells exhibit modifications in nuclear architecture and transcriptional control. Tumor growth and metastasis are supported by RUNX family transcriptional scaffolding proteins, which mediate the assembly of nuclear-matrix-associated gene-regulatory hubs. We used proteomic analysis to identify RUNX2-dependent protein-protein interactions associated with the nuclear matrix in bone, breast and prostate tumor cell types and found that RUNX2 interacts with three distinct proteins that respond to DNA damage - RUVBL2, INTS3 and BAZ1B. Subnuclear foci containing these proteins change in intensity or number following UV irradiation. Furthermore, RUNX2, INTS3 and BAZ1B form UV-responsive complexes with the serine-139-phosphorylated isoform of H2AX (γH2AX). UV irradiation increases the interaction of BAZ1B with γH2AX and decreases histone H3 lysine 9 acetylation levels, which mark accessible chromatin. RUNX2 depletion prevents the BAZ1B-γH2AX interaction and attenuates loss of H3K9 and H3K56 acetylation. Our data are consistent with a model in which RUNX2 forms functional complexes with BAZ1B, RUVBL2 and INTS3 to mount an integrated response to DNA damage. This proposed cytoprotective function for RUNX2 in cancer cells might clarify its expression in chemotherapy-resistant and/or metastatic tumors.

Indexed as

AcetylationATPases Associated with Diverse Cellular ActivitiesBone NeoplasmsBromodomain Containing ProteinsCarrier ProteinsCell Line, TumorCore Binding Factor Alpha 1 SubunitDNA-Binding ProteinsDNA DamageDNA HelicasesDNA RepairHistonesHumansMultiprotein ComplexesOsteosarcomaPhosphorylationATPases Associated with Diverse Cellular ActivitiesBAZ1B protein, humanBromodomain Containing ProteinsCarrier ProteinsCore Binding Factor Alpha 1 SubunitDNA-Binding ProteinsDNA HelicasesH2AX protein, humanHistonesINTS3 protein, humanMultiprotein ComplexesRNA, Small InterferingRUNX2 protein, humanRUVBL2 protein, humanTranscription FactorsBAZ1BBreastCancerDNA damage responseINTS3Nuclear matrixOsteosarcomaProstateProteomicsRUNX2

Identifiers

PMID25609707
PMCPMC4327387
OpenAlexW2070203165

What OpenQuestion holds

Textmetadata
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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.