Evidence map›Paper›PMID 9234731›Full record

ArticleMolecular and cellular biology1997

Muscle LIM protein promotes myogenesis by enhancing the activity of MyoD.

Y Kong, M J Flick, A J Kudla, S F Konieczny

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
9.5field-weighted citation impact, top 1% 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

88 citing papers in PubMed, 287 citations in OpenAlex.

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  11. Role of Muscle LIM Protein in Mechanotransduction Process.International journal of molecular sciences · 2022
    Review
  12. Article
  13. Article
  14. Understanding the molecular basis of cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2022
    Review
  15. Article
  16. Article
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  19. Article
  20. Cysteine- and glycine-rich protein 3 regulates glucose homeostasis in skeletal muscle.American journal of physiology. Endocrinology and metabolism · 2018
    Article

28 more citing papers are in PubMed but not listed here.

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

4 authors at 1 institution in 1 country.

Y KongDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana 47907-1392, USA.
M J Flick
A J Kudla
S F Konieczny
Purdue University West Lafayette · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The muscle LIM protein (MLP) is a muscle-specific LIM-only factor that exhibits a dual subcellular localization, being present in both the nucleus and in the cytoplasm. Overexpression of MLP in C2C12 myoblasts enhances skeletal myogenesis, whereas inhibition of MLP activity blocks terminal differentiation. Thus, MLP functions as a positive developmental regulator, although the mechanism through which MLP promotes terminal differentiation events remains unknown. While examining the distinct roles associated with the nuclear and cytoplasmic forms of MLP, we found that nuclear MLP functions through a physical interaction with the muscle basic helix-loop-helix (bHLH) transcription factors MyoD, MRF4, and myogenin. This interaction is highly specific since MLP does not associate with nonmuscle bHLH proteins E12 or E47 or with the myocyte enhancer factor-2 (MEF2) protein, which acts cooperatively with the myogenic bHLH proteins to promote myogenesis. The first LIM motif in MLP and the highly conserved bHLH region of MyoD are responsible for mediating the association between these muscle-specific factors. MLP also interacts with MyoD-E47 heterodimers, leading to an increase in the DNA-binding activity associated with this active bHLH complex. Although MLP lacks a functional transcription activation domain, we propose that it serves as a cofactor for the myogenic bHLH proteins by increasing their interaction with specific DNA regulatory elements. Thus, the functional complex of MLP-MyoD-E protein reveals a novel mechanism for both initiating and maintaining the myogenic program and suggests a global strategy for how LIM-only proteins may control a variety of developmental pathways.

Indexed as

Transcription FactorsAnimalsCell DifferentiationCell NucleusCytoplasmDimerizationDNA-Binding ProteinsHelix-Loop-Helix MotifsLIM Domain ProteinsMiceMuscle DevelopmentMuscle ProteinsMuscle, SkeletalMyoD ProteinMyogenic Regulatory FactorsMyogenincysteine and glycine-rich protein 3DNA-Binding ProteinsLIM Domain ProteinsMuscle ProteinsMyoD Proteinmyogenic factor 6Myogenic Regulatory FactorsMyogeninMyog protein, mouseMyog protein, ratRecombinant Fusion ProteinsTcf7l1 protein, mouseTcf7l1 protein, ratTCF Transcription FactorsTranscription Factor 7-Like 1 ProteinTranscription Factors

Identifiers

PMID9234731
PMCPMC232327
OpenAlexW2125714022

What OpenQuestion holds

Textmetadata
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.