Evidence map›Paper›PMID 23828041›Full record

ArticleNucleic acids research2013

PP1α, PP1β and Wip-1 regulate H4S47 phosphorylation and deposition of histone H3 variant H3.3.

Hui Zhang, Zhiquan Wang, Zhiguo Zhang

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

7 citing papers in PubMed, 17 citations in OpenAlex.

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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

3 authors at 2 institutions in 1 country.

Hui ZhangDepartment of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, MN 55905, USA.
Zhiquan Wang
Zhiguo Zhang
Mayo Clinic · USWinnMed · US

Funding

Use of microfluidic tumor cultures to enable clinical trials of therapies for ovarian cancerP50CA136393 · NCI · MAYO CLINIC ROCHESTER · PI Zhenkun Lou · 2009 to 2026
$37.0M
Regulation of Nucleosome AssemblyR01GM081838 · NIGMS · MAYO CLINIC ROCHESTER · PI ZHANG, ZHIGUO · 2008 to 2015
$2.4M
The role of a histone H4 phosphorylation in drug resistanceR01CA157489 · NCI · MAYO CLINIC ROCHESTER · PI ZHANG, ZHIGUO · 2012 to 2016
$1.6M
NCI NIH HHS CA157489NCI NIH HHS P50 CA136393NCI NIH HHS R01 CA157489NIGMS NIH HHS GM81838NIGMS NIH HHS R01 GM081838
6 · The paper itself

Abstract

Phosphorylation of histone H4 serine 47 (H4S47ph) is catalyzed by Pak2, a member of the p21-activated serine/threonine protein kinase (Pak) family and regulates the deposition of histone variant H3.3. However, the phosphatase(s) involved in the regulation of H4S47ph levels was unknown. Here, we show that three phosphatases (PP1α, PP1β and Wip1) regulate H4S47ph levels and H3.3 deposition. Depletion of each of the three phosphatases results in increased H4S47ph levels. Moreover, PP1α, PP1β and Wip1 bind H3-H4 in vitro and in vivo, whereas only PP1α and PP1β, but not Wip1, interact with Pak2 in vivo. These results suggest that PP1α, PP1β and Wip1 regulate the levels of H4S47ph through directly acting on H4S47ph, with PP1α and PP1β also likely regulating the activity of Pak2. Finally, depletion of PP1α, PP1β and Wip1 leads to increased H3.3 occupancy at candidate genes tested, elevated H3.3 deposition and enhanced association of H3.3 with its chaperones HIRA and Daxx. These results reveal a novel role of three phosphatases in chromatin dynamics in mammalian cells.

Indexed as

Adaptor Proteins, Signal TransducingCell Cycle ProteinsCell LineCo-Repressor ProteinsHeLa CellsHistone ChaperonesHistonesHumansMolecular ChaperonesNuclear Proteinsp21-Activated KinasesPhosphoprotein PhosphatasesPhosphorylationProtein Phosphatase 1Protein Phosphatase 2CSerineAdaptor Proteins, Signal TransducingCell Cycle ProteinsCo-Repressor ProteinsDAXX protein, humanHIRA protein, humanHistone ChaperonesHistonesMolecular ChaperonesNuclear Proteinsp21-Activated KinasesPAK2 protein, humanPhosphoprotein PhosphatasesPPM1D protein, humanProtein Phosphatase 1Protein Phosphatase 2CSerineTranscription Factors

Identifiers

PMID23828041
PMCPMC3783166
OpenAlexW2004585206

What OpenQuestion holds

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LicenceCC BY-NC
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.