Evidence map›Paper›PMID 28057922›Full record

ArticleScientific reports2017

Membrane translocation of t-SNARE protein syntaxin-4 abrogates ground-state pluripotency in mouse embryonic stem cells.

Natsumi Hagiwara-Chatani, Kota Shirai, Takumi Kido, Tomoatsu Horigome, Akihiro Yasue, Naoki Adachi, Yohei Hirai

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 41% 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

4 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. The Janus-faced functions of Apolipoproteins L in membrane dynamics.Cellular and molecular life sciences : CMLS · 2024
    Article
  3. Article
  4. Review
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 2 institutions in 1 country.

Natsumi Hagiwara-ChataniDepartment of Biomedical Chemistry, Graduate School of Science and Technology, Kwansei Gakuin University, Sanda, Japan.
Kota ShiraiDepartment of Biomedical Chemistry, Graduate School of Science and Technology, Kwansei Gakuin University, Sanda, Japan.
Takumi KidoDepartment of Biomedical Chemistry, Graduate School of Science and Technology, Kwansei Gakuin University, Sanda, Japan.
Tomoatsu HorigomeDepartment of Biomedical Chemistry, Graduate School of Science and Technology, Kwansei Gakuin University, Sanda, Japan.
Akihiro YasueDepartment of Orthodontics and Dentofacial Orthopedics, Institute of Health Biosciences, The University of Tokushima, Tokushima, Japan.
Naoki AdachiDepartment of Biomedical Chemistry, Graduate School of Science and Technology, Kwansei Gakuin University, Sanda, Japan.
Yohei HiraiDepartment of Biomedical Chemistry, Graduate School of Science and Technology, Kwansei Gakuin University, Sanda, Japan.
Kwansei Gakuin University · JPTokushima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Embryonic stem (ES) and induced pluripotent stem (iPS) cells are attractive tools for regenerative medicine therapies. However, aberrant cell populations that display flattened morphology and lose ground-state pluripotency often appear spontaneously, unless glycogen synthase kinase 3β (GSK3β) and mitogen-activated protein kinase kinase (MEK1/2) are inactivated. Here, we show that membrane translocation of the t-SNARE protein syntaxin-4 possibly is involved in this phenomenon. We found that mouse ES cells cultured without GSK3β/MEK1/2 inhibitors (2i) spontaneously extrude syntaxin-4 at the cell surface and that artificial expression of cell surface syntaxin-4 induces appreciable morphological changes and mesodermal differentiation through dephosphorylation of Akt. Transcriptome analyses revealed several candidate elements responsible for this, specifically, an E-to P-cadherin switch and a marked downregulation of Zscan4 proteins, which are DNA-binding proteins essential for ES cell pluripotency. Embryonic carcinoma cell lines F9 and P19CL6, which maintain undifferentiated states independently of Zscan4 proteins, exhibited similar cellular behaviors upon stimulation with cell surface syntaxin-4. The functional ablation of E-cadherin and overexpression of P-cadherin reproduced syntaxin-4-induced cell morphology, demonstrating that the E- to P-cadherin switch executes morphological signals from cell surface syntaxin-4. Thus, spontaneous membrane translocation of syntaxin-4 emerged as a critical element for maintenance of the stem-cell niche.

Indexed as

Cell DifferentiationAnimalsCadherinsCell LineCell MembraneCulture MediaEmbryonic Stem CellsGlycogen Synthase Kinase 3 betaMAP Kinase Kinase 1MAP Kinase Kinase 2MiceProtein Kinase InhibitorsProto-Oncogene Proteins c-aktQa-SNARE ProteinsStem Cell NicheTranscriptomeCadherinsCulture MediaGlycogen Synthase Kinase 3 betaMap2k2 protein, mouseMAP Kinase Kinase 1MAP Kinase Kinase 2Protein Kinase InhibitorsProto-Oncogene Proteins c-aktQa-SNARE Proteins

Identifiers

PMID28057922
PMCPMC5216394
OpenAlexW2568164787

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.