Evidence map›Paper›PMID 24901984›Full record

ArticlePLoS genetics2014

Glycogen synthase kinase (GSK) 3β phosphorylates and protects nuclear myosin 1c from proteasome-mediated degradation to activate rDNA transcription in early G1 cells.

Aishe A Sarshad, Martin Corcoran, Bader Al-Muzzaini, Laura Borgonovo-Brandter, Anne Von Euler, Douglas Lamont, Neus Visa, Piergiorgio Percipalle

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

13 citing papers in PubMed, 31 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

8 authors at 3 institutions in 2 countries.

Aishe A SarshadDepartment of Cell and Molecular Biology, Karolinska Institute, Stockholm, Sweden.
Martin CorcoranDepartment of Cell and Molecular Biology, Karolinska Institute, Stockholm, Sweden.
Bader Al-MuzzainiDepartment of Cell and Molecular Biology, Karolinska Institute, Stockholm, Sweden.
Laura Borgonovo-BrandterDepartment of Cell and Molecular Biology, Karolinska Institute, Stockholm, Sweden.
Anne Von EulerDepartment of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Stockholm, Sweden.
Douglas LamontFingerPrints Proteomics Facility, College of Life Sciences, University of Dundee, Dundee, United Kingdom.
Neus VisaDepartment of Molecular Biosciences, The Wenner-Gren Institute, Stockholm University, Stockholm, Sweden.
Piergiorgio PercipalleDepartment of Cell and Molecular Biology, Karolinska Institute, Stockholm, Sweden.
Karolinska Institutet · SEStockholm University · SEUniversity of Dundee · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nuclear myosin 1c (NM1) mediates RNA polymerase I (pol I) transcription activation and cell cycle progression by facilitating PCAF-mediated H3K9 acetylation, but the molecular mechanism by which NM1 is regulated remains unclear. Here, we report that at early G1 the glycogen synthase kinase (GSK) 3β phosphorylates and stabilizes NM1, allowing for NM1 association with the chromatin. Genomic analysis by ChIP-Seq showed that this mechanism occurs on the rDNA as active GSK3β selectively occupies the gene. ChIP assays and transmission electron microscopy in GSK3β-/- mouse embryonic fibroblasts indicated that at G1 rRNA synthesis is suppressed due to decreased H3K9 acetylation leading to a chromatin state incompatible with transcription. We found that GSK3β directly phosphorylates the endogenous NM1 on a single serine residue (Ser-1020) located within the NM1 C-terminus. In G1 this phosphorylation event stabilizes NM1 and prevents NM1 polyubiquitination by the E3 ligase UBR5 and proteasome-mediated degradation. We conclude that GSK3β-mediated phosphorylation of NM1 is required for pol I transcription activation.

Indexed as

AcetylationAnimalsCell LineChromatinDNA, RibosomalF-Box ProteinsG1 PhaseGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaHEK293 CellsHeLa CellsHistonesHumansMiceMice, KnockoutMyosin Type IChromatinDNA, RibosomalF-Box ProteinsFBXW8 protein, humanGlycogen Synthase Kinase 3Glycogen Synthase Kinase 3 betaGSK3B protein, humanGsk3b protein, mouseHistonesMYO1C protein, humanMyosin Type Ip300-CBP-Associated Factorp300-CBP Transcription FactorsRNA Polymerase IRNA, Small InterferingUbiquitin-Protein LigasesUBR5 protein, human

Identifiers

PMID24901984
PMCPMC4046919
OpenAlexW1993168446

What OpenQuestion holds

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LicenceCC BY
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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.