Evidence map›Paper›PMID 28607151›Full record

ArticleThe Journal of biological chemistry2017

The transcriptional co-repressor TLE3 regulates myogenic differentiation by repressing the activity of the MyoD transcription factor.

Shoichiro Kokabu, Chihiro Nakatomi, Takuma Matsubara, Yusuke Ono, William N Addison, Jonathan W Lowery, Mariko Urata, Aaron M Hudnall, Suzuro Hitomi, Mitsushiro Nakatomi and 5 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed, 38 citations in OpenAlex.

  1. Article
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  8. Zeb1 and Tle3 are trans-factors that differentially regulate the expression of myosin heavy chain-embryonic and skeletal muscle differentiation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2023
    Article
  9. Article
  10. Effects of Myostatin on Nuclear Morphology at the Myotendinous Junction.International journal of molecular sciences · 2023
    Article
  11. Review
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  18. TCF21: a critical transcription factor in health and cancer.Journal of molecular medicine (Berlin, Germany) · 2020
    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

15 authors at 7 institutions in 3 countries.

Shoichiro KokabuDivisions of Molecular Signaling and Biochemistry, Kyushu Dental University, Kitakyushu 803-8580, Japan; Department of Oral and Maxillofacial Surgery, Faculty of Medicine, Saitama Medical University, Moroyama-machi, Iruma-gun, Saitama 350-0495, Japan; Department of Developmental Biology, Harvard School of Dental Medicine, Boston, Massachusetts 02115. Electronic address: r14kokabu@fa.kyu-dent.ac.jp.
Chihiro NakatomiDivisions of Molecular Signaling and Biochemistry, Kyushu Dental University, Kitakyushu 803-8580, Japan.
Takuma MatsubaraDivisions of Molecular Signaling and Biochemistry, Kyushu Dental University, Kitakyushu 803-8580, Japan.
Yusuke OnoMusculoskeletal Molecular Biology Research Group, Nagasaki University Graduate School of Biomedical Sciences, Nagasaki 852-8102, Japan.
William N AddisonResearch Unit, Department of Human Genetics, Shriners Hospitals for Children, McGill University, Montreal, Quebec H4A 0A9, Canada.
Jonathan W LoweryDivision of Biomedical Science, College of Osteopathic Medicine, Marian University, Indianapolis, Indiana 46222.
Mariko UrataDivisions of Molecular Signaling and Biochemistry, Kyushu Dental University, Kitakyushu 803-8580, Japan.
Aaron M HudnallDivision of Biomedical Science, College of Osteopathic Medicine, Marian University, Indianapolis, Indiana 46222.
Suzuro HitomiDivision of Physiology, Kyushu Dental University, Kitakyushu 803-8580, Japan.
Mitsushiro NakatomiDivision of Anatomy, Department of Health Promotion, Kyushu Dental University, Kitakyushu 803-8580, Japan.
Tsuyoshi SatoDepartment of Oral and Maxillofacial Surgery, Faculty of Medicine, Saitama Medical University, Moroyama-machi, Iruma-gun, Saitama 350-0495, Japan.
Kenji OsawaDivision of Oral Medicine, Department of Science of Physical Functions, Kyushu Dental University, Kitakyushu 803-8580, Japan.
Tetsuya YodaDepartment of Oral and Maxillofacial Surgery, Faculty of Medicine, Saitama Medical University, Moroyama-machi, Iruma-gun, Saitama 350-0495, Japan.
Vicki RosenDepartment of Developmental Biology, Harvard School of Dental Medicine, Boston, Massachusetts 02115.
Eijiro JimiDivisions of Molecular Signaling and Biochemistry, Kyushu Dental University, Kitakyushu 803-8580, Japan; Oral Health Brain Health Total Health, Laboratory of Molecular and Cellular Biochemistry, Faculty of Dental Science, Kyushu University, Fukuoka 812-8582, Japan.
Kyushu Dental University · JPSaitama Medical University · JPMarian University - Indiana · USHarvard University · USKyushu University · JPMcGill University · CANagasaki University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Satellite cells are skeletal muscle stem cells that provide myonuclei for postnatal muscle growth, maintenance, and repair/regeneration in adults. Normally, satellite cells are mitotically quiescent, but they are activated in response to muscle injury, in which case they proliferate extensively and exhibit up-regulated expression of the transcription factor MyoD, a master regulator of myogenesis. MyoD forms a heterodimer with E proteins through their basic helix-loop-helix domain, binds to E boxes in the genome and thereby activates transcription at muscle-specific promoters. The central role of MyoD in muscle differentiation has increased interest in finding potential MyoD regulators. Here we identified transducin-like enhancer of split (TLE3), one of the Groucho/TLE family members, as a regulator of MyoD function during myogenesis. TLE3 was expressed in activated and proliferative satellite cells in which increased TLE3 levels suppressed myogenic differentiation, and, conversely, reduced TLE3 levels promoted myogenesis with a concomitant increase in proliferation. We found that, via its glutamine- and serine/proline-rich domains, TLE3 interferes with MyoD function by disrupting the association between the basic helix-loop-helix domain of MyoD and E proteins. Our findings indicate that TLE3 participates in skeletal muscle homeostasis by dampening satellite cell differentiation via repression of MyoD transcriptional activity.

Indexed as

Gene Expression Regulation, DevelopmentalMuscle DevelopmentActivating Transcription Factor 3AnimalsCell ProliferationCells, CulturedCo-Repressor ProteinsGene DeletionHelix-Loop-Helix MotifsMaleMiceMice, Inbred C57BLMuscle Fibers, SkeletalMyoblastsMyoD ProteinPeptide FragmentsActivating Transcription Factor 3Atf3 protein, mouseCo-Repressor ProteinsMyoD1 myogenic differentiation proteinMyoD ProteinPeptide FragmentsRecombinant Fusion ProteinsRecombinant ProteinsTle3 protein, mousebasic helix-loop-helix (bHLH) transcription factormesenchymal stem cells (MSCs)MyoDmyogenesisskeletal muscleTLE

Identifiers

PMID28607151
PMCPMC5546029
OpenAlexW2626387809

What OpenQuestion holds

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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.