Evidence map›Paper›PMID 21646345›Full record

ArticleThe Journal of biological chemistry2011

Phosphorylation of histone H2B serine 32 is linked to cell transformation.

Andy T Y Lau, Sung-Young Lee, Yan-Ming Xu, Duo Zheng, Yong-Yeon Cho, Feng Zhu, Hong-Gyum Kim, Sheng-Qing Li, Zhiguo Zhang, Ann M Bode and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

28 citing papers in PubMed, 47 citations in OpenAlex.

  1. Review
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  3. Targeting RSK2 in Cancer Therapy: A Review of Natural Products.Anti-cancer agents in medicinal chemistry · 2025
    Review
  4. Article
  5. Epigenetic Regulation of EMP/EMT-Dependent Fibrosis.International journal of molecular sciences · 2024
    Review
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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 3 institutions in 2 countries.

Andy T Y LauHormel Institute, University of Minnesota, Austin, Minnesota 55912, USA.
Sung-Young Lee
Yan-Ming Xu
Duo Zheng
Yong-Yeon Cho
Feng Zhu
Hong-Gyum Kim
Sheng-Qing Li
Zhiguo Zhang
Ann M Bode
Zigang Dong
Hormel (United States) · USUniversity of Minnesota · USMayo Clinic · US

Funding

Ultraviolet-Induced Signal TrasductionR01CA077646 · NCI · UNIVERSITY OF MINNESOTA TWIN CITIES · PI DONG, ZIGANG · 1999 to 2010
$2.3M
The role of histone phosphorylation in arsenic-induced cell transformation and skR01ES016548 · NIEHS · UNIVERSITY OF MINNESOTA · PI DONG, ZIGANG · 2008 to 2012
$1.7M
Anticarcinogenic Mechanisms of Tea ConstituentsR37CA081064 · NCI · UNIVERSITY OF MINNESOTA · PI DONG, ZIGANG · 2008 to 2012
$1.5M
Inhibition of Carcinogenesis by Tea and Tea ConstituentsR01CA120388 · NCI · UNIVERSITY OF MINNESOTA · PI DONG, ZIGANG · 2006 to 2010
$1.3M
NCI NIH HHS CA077646NCI NIH HHS CA120388NCI NIH HHS R01 CA077646NCI NIH HHS R01 CA120388NCI NIH HHS R37 CA081064NCI NIH HHS R37CA081064NIEHS NIH HHS ES016548NIEHS NIH HHS R01 ES016548
6 · The paper itself

Abstract

Various types of post-translational modifications of the histone tails have been revealed, but a few modifications have been found within the histone core sequences. Histone core post-translational modifications have the potential to modulate nucleosome structure and DNA accessibility. Here, we studied the histone H2B core domain and found that phosphorylation of H2B serine 32 occurs in normal cycling and mitogen-stimulated cells. Notably, this phosphorylation is elevated in skin cancer cell lines and tissues compared with normal counterparts. The JB6 Cl41 mouse skin epidermal cell line is a well established model for tumor promoter-induced cell transformation and was used to study the function of H2B during EGF-induced carcinogenesis. Remarkably, cells overexpressing a nonphosphorylatable H2BS32A mutant exhibited suppressed growth and EGF-induced cell transformation, possibly because of decreased activation of activator protein-1, compared with control cells overexpressing wild type H2B. We identified ribosomal S6 kinase 2 (RSK2) as the kinase responsible for H2BS32 phosphorylation. Serum-starved JB6 cells contain very little endogenous H2BS32 phosphorylation, and EGF treatment induced this phosphorylation. The phosphorylation was attenuated in RSK2 knock-out MEFs and RSK2 knockdown JB6 cells. Taken together, our results demonstrate a novel role for H2B phosphorylation in cell transformation and show that H2BS32 phosphorylation is critical for controlling activator protein-1 activity, which is a major driver in cell transformation.

Indexed as

Amino Acid SubstitutionAnimalsCell Transformation, NeoplasticEpidermal Growth FactorEpidermisHEK293 CellsHistonesHumansMiceMice, KnockoutMutation, MissensePhosphorylationRibosomal Protein S6 Kinases, 90-kDaSerineTranscription Factor AP-1Epidermal Growth FactorHistonesribosomal protein S6 kinase, 90kDa, polypeptide 3Ribosomal Protein S6 Kinases, 90-kDaSerineTranscription Factor AP-1

Identifiers

PMID21646345
PMCPMC3143627
OpenAlexW2068125777

What OpenQuestion holds

Textmetadata
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.