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Updated: Feb 8, 2026
06:44
Age-dependent Dynamics of Locomotion in Caenorhabditis elegans: A Lyapunov Exponent Analysis
Published on: September 23, 2025
578
Solution structure and dynamics of glia maturation factor from Caenorhabditis elegans
Diva Maheshwari1, Vaibhav Kumar Shukla2, Anupam Jain2
1Molecular and Structural Biology Division, CSIR-Central Drug Research Institute, Lucknow 226031, India; Academy of Scientific and Innovative Research, New Delhi 110025, India.
Summary
This study presents the first solution structure of CeGMF, revealing structural differences compared to mammalian GMF. These findings offer insights into GMF
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Dynamics
Background:
- GMF proteins regulate actin dynamics by interacting with the Arp2/3 complex and F-actin.
- CeGMF from C. elegans shares homology with human and mouse GMFγ.
Purpose of the Study:
- To characterize the solution structure, dynamics, and thermal stability of CeGMF.
- To elucidate structural differences between CeGMF and mammalian GMF isoforms.
Main Methods:
- Solution NMR spectroscopy for structure and dynamics.
- Differential Scanning Calorimetry (DSC) for thermal stability.
Main Results:
- CeGMF exhibits a canonical ADF-H fold with unique structural features in the β4-β5 loop.
- Site-1 shows dynamic flexibility, while Site-2's β4-β5 loop has reduced flexibility compared to ADF/cofilin.
- CeGMF displays significantly higher thermal stability than ADF/cofilin homologs.
Conclusions:
- The study provides the first solution structure of CeGMF, highlighting structural distinctions in Site-2 compared to mammalian GMF.
- Differences in structure, dynamics, and thermal stability distinguish GMF from ADF/cofilin proteins.
- Insights into structural and dynamic factors governing GMF specificity for the Arp2/3 complex.
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