Evidence map›Paper›PMID 25306110›Full record

ArticleNature structural & molecular biology2014

MacroH2A1.1 and PARP-1 cooperate to regulate transcription by promoting CBP-mediated H2B acetylation.

Hongshan Chen, Penelope D Ruiz, Leonid Novikov, Alyssa D Casill, Jong Woo Park, Matthew J Gamble

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

80 citing papers in PubMed, 111 citations in OpenAlex.

  1. Article
  2. Splice isoforms of the histone variant macroH2A1 differentially regulate hippocampal gene expression and memory formation.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2026
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  18. Histone H2A variants: Diversifying chromatin to ensure genome integrity.Seminars in cell & developmental biology · 2023
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  20. Article

20 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 2 institutions in 2 countries.

Hongshan ChenDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, Yeshiva University, Bronx, New York, USA.
Penelope D RuizDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, Yeshiva University, Bronx, New York, USA.
Leonid NovikovDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, Yeshiva University, Bronx, New York, USA.
Alyssa D CasillDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, Yeshiva University, Bronx, New York, USA.
Jong Woo ParkDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, Yeshiva University, Bronx, New York, USA.
Matthew J GambleDepartment of Molecular Pharmacology, Albert Einstein College of Medicine, Yeshiva University, Bronx, New York, USA.
Albert Einstein College of Medicine · USYeshiva University · US

Funding

WORD PROCESSORP30CA013330 · NCI · YESHIVA UNIVERSITY · PI THOMAS E ROHAN · 1985 to 2026
$111.2M
TRAINING PROGRAM IN CELLULAR &MOLEC. BIOLOGY &GENETICST32GM007491 · NIGMS · YESHIVA UNIVERSITY · PI QUERY, CHARLES C · 1985 to 2021
$17.0M
The role of macroH2A variants in cancer and senescenceR01CA155232 · NCI · ALBERT EINSTEIN COLLEGE OF MEDICINE, INC · PI GAMBLE, MATTHEW J · 2012 to 2021
$3.7M
NCI NIH HHS P30 CA013330NCI NIH HHS R01 CA155232NCI NIH HHS R01CA155232NIGMS NIH HHS T32 GM007491NIGMS NIH HHS T32GM007491-38
6 · The paper itself

Abstract

The histone variant macroH2A1 regulates gene expression important for differentiation, stem-cell reprogramming and tumor suppression. Here, we demonstrate that in primary human cells, macroH2A1 participates in two physically and functionally distinct types of chromatin marked by either H3K27me3 or nine histone acetylations. Using RNA sequencing, we found that macroH2A1-regulated genes, which have roles in cancer progression, are specifically found in macroH2A1-containing acetylated chromatin. Of the two macroH2A1 variants, macroH2A1.1 and macroH2A1.2, the former is suppressed in cancer and can interact with PARP-generated poly(ADP-ribose). Through the recruitment of PARP-1, macroH2A1.1 promotes the CBP-mediated acetylation of H2B K12 and K120, which either positively or negatively regulates the expression of macroH2A1-target genes. Although macroH2A1-regulated H2B acetylation is a common feature of primary cells, this regulation is typically lost in cancer cells. Consequently, our results provide insight into macroH2A1.1's role in cancer suppression.

Indexed as

Gene Expression Regulation, NeoplasticTranscription, GeneticAcetylationBinding SitesCell Line, TransformedCell Line, TumorChromatinFetusFibroblastsHistonesHumansLungPeptide FragmentsPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesProtein Bindingbone sialoprotein (35-62), humanChromatinHistonesmacroH2A histonePARP1 protein, humanPeptide FragmentsPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) PolymerasesProtein IsoformsSialoglycoproteins

Identifiers

PMID25306110
PMCPMC4221384
OpenAlexW2002670570

What OpenQuestion holds

Textmetadata
LicenceTDM
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.