Evidence map›Paper›PMID 20855292›Full record

ArticleNucleic acids research2011

Dual-specificity phosphatase 23 mediates GCM1 dephosphorylation and activation.

Fang-Yu Lin, Ching-Wen Chang, Mei-Leng Cheong, Hsei-Chorn Chen, Der-Yen Lee, Geen-Dong Chang, Hungwen Chen

Open access · goldAbstract read
In one paragraph

Article in Nucleic acids research, 2011. 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
1.3field-weighted citation impact, top 18% 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, 31 citations in OpenAlex.

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  6. The multifaceted role of GCM1 during trophoblast differentiation in the human placenta.Proceedings of the National Academy of Sciences of the United States of America · 2022
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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

7 authors at 3 institutions in 1 country.

Fang-Yu LinGraduate Institute of Biochemical Sciences, National Taiwan University, Nankang, Taipei 115, Taiwan.
Ching-Wen Chang
Mei-Leng Cheong
Hsei-Chorn Chen
Der-Yen Lee
Geen-Dong Chang
Hungwen Chen
Cathay General Hospital · TWNational Taiwan University · TWInstitute of Biological Chemistry, Academia Sinica · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glial cells missing homolog 1 (GCM1) is a transcription factor essential for placental development. GCM1 promotes syncytiotrophoblast formation and placental vasculogenesis by activating fusogenic and proangiogenic gene expression in placenta. GCM1 activity is regulated by multiple post-translational modifications. The cAMP/PKA-signaling pathway promotes CBP-mediated GCM1 acetylation and stabilizes GCM1, whereas hypoxia-induced GSK-3β-mediated phosphorylation of Ser322 causes GCM1 ubiquitination and degradation. How and whether complex modifications of GCM1 are coordinated is not known. Here we show that the interaction of GCM1 and dual-specificity phosphatase 23 (DUSP23) is enhanced by PKA-dependent phosphorylation of GCM1 on Ser269 and Ser275. The recruitment of DUSP23 reverses GSK-3β-mediated Ser322 phosphorylation, which in turn promotes GCM1 acetylation, stabilization and activation. Supporting a central role in coordinating GCM1 modifications, knockdown of DUSP23 suppressed GCM1 target gene expression and placental cell fusion. Our study identifies DUSP23 as a novel factor that promotes placental cell fusion and reveals a complex regulation of GCM1 activity by coordinated phosphorylation, dephosphorylation and acetylation.

Indexed as

AcetylationCell FusionCell LineCyclic AMPCyclic AMP-Dependent Protein KinasesDNA-Binding ProteinsDual-Specificity PhosphatasesHumansNuclear ProteinsPhosphorylationSerineTranscription FactorsTrophoblastsUbiquitinationCyclic AMPCyclic AMP-Dependent Protein KinasesDNA-Binding ProteinsDual-Specificity PhosphatasesDUSP23 protein, humanGCM1 protein, humanNuclear ProteinsSerineTranscription Factors

Identifiers

PMID20855292
PMCPMC3035457
OpenAlexW2040284079

What OpenQuestion holds

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LicenceCC BY-NC
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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.