Evidence map›Paper›PMID 19812254›Full record

ArticleMolecular biology of the cell2009

Neogenin regulates skeletal myofiber size and focal adhesion kinase and extracellular signal-regulated kinase activities in vivo and in vitro.

Gyu-Un Bae, Youn-Joo Yang, Guoying Jiang, Mingi Hong, Hye-Jin Lee, Marc Tessier-Lavigne, Jong-Sun Kang, Robert S Krauss

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed, 1 pooled it
2.6field-weighted citation impact, top 11% 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

38 citing papers in PubMed, 1 synthesis or guideline pooled it, 64 citations in OpenAlex.

  1. Pooled it
  2. Article
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  9. Article
  10. eLife · 2020
    Article
  11. Neogenin-1 distinguishes between myeloid-biased and balancedProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Keep Your Friends Close: Cell-Cell Contact and Skeletal Myogenesis.Cold Spring Harbor perspectives in biology · 2017
    Review
  17. Article
  18. Article
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  20. Article
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 2 institutions in 2 countries.

Gyu-Un BaeDepartment of Developmental and Regenerative Biology, Mount Sinai School of Medicine, New York, NY 10029, USA
Youn-Joo Yang
Guoying Jiang
Mingi Hong
Hye-Jin Lee
Marc Tessier-Lavigne
Jong-Sun Kang
Robert S Krauss
Samsung (South Korea) · KRIcahn School of Medicine at Mount Sinai · US

Funding

THE ROLE OF CDO IN MYOGENIC DIFFERENTIATIONR01AR046207 · NIAMS · MOUNT SINAI SCHOOL OF MEDICINE OF NYU · PI KRAUSS, ROBERT S. · 2000 to 2015
$5.1M
NIAMS NIH HHS AR46207NIAMS NIH HHS R01 AR046207
6 · The paper itself

Abstract

A variety of signaling pathways participate in the development of skeletal muscle, but the extracellular cues that regulate such pathways in myofiber formation are not well understood. Neogenin is a receptor for ligands of the netrin and repulsive guidance molecule (RGM) families involved in axon guidance. We reported previously that neogenin promoted myotube formation by C2C12 myoblasts in vitro and that the related protein Cdo (also Cdon) was a potential neogenin coreceptor in myoblasts. We report here that mice homozygous for a gene-trap mutation in the Neo1 locus (encoding neogenin) develop myotomes normally but have small myofibers at embryonic day 18.5 and at 3 wk of age. Similarly, cultured myoblasts derived from such animals form smaller myotubes with fewer nuclei than myoblasts from control animals. These in vivo and in vitro defects are associated with low levels of the activated forms of focal adhesion kinase (FAK) and extracellular signal-regulated kinase (ERK), both known to be involved in myotube formation, and inefficient expression of certain muscle-specific proteins. Recombinant netrin-2 activates FAK and ERK in cultured myoblasts in a neogenin- and Cdo-dependent manner, whereas recombinant RGMc displays lesser ability to activate these kinases. Together, netrin-neogenin signaling is an important extracellular cue in regulation of myogenic differentiation and myofiber size.

Indexed as

AnimalsCadherinsCell DifferentiationCells, CulturedDesminEmbryo, MammalianEnzyme ActivationExtracellular Signal-Regulated MAP KinasesFocal Adhesion Protein-Tyrosine KinasesMembrane ProteinsMiceMice, Inbred C57BLMice, TransgenicMorphogenesisMuscle, SkeletalMutationCadherinsDesminExtracellular Signal-Regulated MAP KinasesFocal Adhesion Protein-Tyrosine KinasesMembrane ProteinsMyogeninneogeninNerve Growth Factorsnetrin-2NetrinsRecombinant Fusion Proteins

Identifiers

PMID19812254
PMCPMC2785735
OpenAlexW2002523663

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.