Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways

Rommel C, Bodine SC, Clarke BA, Rossman R, Nunez L, Stitt TN, Yancopoulos GD, Glass DJ · 2001 · Nature Cell Biology · Atlas ID ROM2001

What this study shows

Shows IGF-1 drives muscle fiber hypertrophy through Akt, via both the mTOR and GSK3 branches, in cultured myotubes, establishing mTOR as a central node for muscle growth signaling.

Abstract

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Skeletal muscle is composed of multinucleated fibres, formed after the differentiation and fusion of myoblast precursors. Skeletal muscle atrophy and hypertrophy refer to changes in the diameter of these pre-existing muscle fibres. The prevention of atrophy would provide an obvious clinical benefit; insulin-like growth factor 1 (IGF-1) is a promising anti-atrophy agent because of its ability to promote hypertrophy.

Read the full abstract on PubMed →

At a glance

Evidence type	M Molecular — cells, biochemistry, structure Marked M because it is molecular or in-vitro work (model: Cultured muscle cells (mouse)) rather than a whole-organism health-outcome study. That is often exactly where causal biology gets established -- the code says which system the finding was shown in, and nothing about how good the work is.
Study type	5 - Mechanistic / In Vitro
Model system	Cultured muscle cells (mouse)
Journal	Nature Cell Biology
Year	2001
Peer reviewed	Yes
Record last updated	2026-10-01
Source	DOI 10.1038/ncb1101-1009 · PMID 11715022

Extracted findings

These fields were extracted from the paper with AI assistance and have not been checked against the source. Read them as a pointer into the paper, not as curated claims; where they disagree with the curated summary above, the curated summary stands.

Intervention	IGF-1
Target	PI3K/Akt/mTOR & Akt/GSK3
Model	Cultured muscle cells (mouse)
Effect	IGF-1 drives skeletal myotube hypertrophy via PI3K/Akt/mTOR and PI3K/Akt/GSK3 pathways

In the Atlas

Links in the pathway map

Supports Growth hormone / IGF-1 axis activates PI3K
Supports Protein synthesis activates Muscle growth

Open questions that cite this study

Cited as supporting evidence for the open question Muscle-sparing, pulsed mTORC1 inhibition.

Cite this paper

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Rommel, C., Bodine, S. C., Clarke, B. A., Rossman, R., Nunez, L., Stitt, T. N., Yancopoulos, G. D., & Glass, D. J. (2001). Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways. Nature Cell Biology. https://doi.org/10.1038/ncb1101-1009

@article{ROM2001,
  author       = {Rommel, C. and Bodine, S. C. and Clarke, B. A. and Rossman, R. and Nunez, L. and Stitt, T. N. and Yancopoulos, G. D. and Glass, D. J.},
  title        = {{Mediation of IGF-1-induced skeletal myotube hypertrophy by PI(3)K/Akt/mTOR and PI(3)K/Akt/GSK3 pathways}},
  journal      = {Nature Cell Biology},
  year         = {2001},
  doi          = {10.1038/ncb1101-1009},
  note         = {PMID: 11715022},
}

Cite this Atlas record

The record is the Atlas's own work — the evidence label, the extracted findings and the links. It is cited as part of the dataset, not as the paper.

Barton, O. (2026). Oliver's mTOR Atlas (record ROM2001) [Data set]. https://mtor-atlas.org/study/ROM2001/ · Dataset DOI 10.5281/zenodo.22059963

@misc{atlas_ROM2001,
  author       = {Barton, Oliver},
  title        = {{Oliver's mTOR Atlas}, record ROM2001},
  howpublished = {Data set},
  year         = {2026},
  url          = {https://mtor-atlas.org/study/ROM2001/},
  doi          = {10.5281/zenodo.22059963}
}

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