Related Experiment Video
Updated: Jun 17, 2026
14:36
Adult and Embryonic Skeletal Muscle Microexplant Culture and Isolation of Skeletal Muscle Stem Cells
Published on: September 21, 2010
Translational control by DHX36 binding to 5'UTR G-quadruplex is essential for muscle stem-cell regenerative functions
Xiaona Chen1, Jie Yuan2, Guang Xue1
1Department of Orthopaedics and Traumatology, Li Ka Shing Institute of Health Sciences, Chinese University of Hong Kong, Hong Kong SAR, China.
Nature Communications
|August 20, 2021
Summary
DHX36, an RNA helicase, is crucial for skeletal muscle regeneration by controlling satellite cell expansion. It unwinds RNA G-quadruplex structures, promoting the translation of key mRNAs essential for muscle repair.
Area of Science:
- Molecular Biology
- Cell Biology
- Regenerative Medicine
Background:
- Skeletal muscle regeneration relies on resident satellite cells (SCs).
- The molecular mechanisms governing SC proliferation during regeneration are not fully understood.
- RNA G-quadruplex (rG4) structures can regulate gene expression post-transcriptionally.
Purpose of the Study:
- To investigate the role of the RNA helicase DHX36 in skeletal muscle regeneration.
- To elucidate the mechanism by which DHX36 regulates SC proliferation.
Main Methods:
- Inducible deletion of Dhx36 in adult mouse SCs.
- System-wide mapping of DHX36 binding sites.
- Integrated polysome profiling to assess mRNA translation.
- Analysis of Gnai2 mRNA translation regulation.
Main Results:
- DHX36 expression is induced during SC activation and proliferation.
- Deletion of Dhx36 impairs SC proliferation and muscle regeneration.
- DHX36 binds to rG4 structures in mRNA 5'-untranslated regions (UTRs).
- DHX36 promotes mRNA translation by unwinding 5'-UTR rG4s, specifically regulating Gnai2 mRNA.
Conclusions:
- DHX36 is essential for skeletal muscle regeneration by controlling SC expansion.
- DHX36 acts as a post-transcriptional regulator, unwinding rG4 structures to enhance translation of specific mRNAs.
- GNAI2 is identified as a key downstream effector of DHX36 in SCs.
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