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Updated: Aug 6, 2026
12:35
Optogenetic Inhibition of Rho1-Mediated Actomyosin Contractility Coupled with Measurement of Epithelial Tension in Drosophila Embryos
Published on: April 14, 2023
Reversible Actin modifications by Mical and SelR regulate dynamic actomyosin ring functions during cell wound repair
Biorxiv : the Preprint Server for Biology
|July 17, 2026
Summary
A novel Rab35-Mical-SelR pathway controls cell wound repair by regulating actin redox state. This pathway is crucial for the dynamic assembly and disassembly of the actomyosin ring, ensuring proper cell repair.
Area of Science:
- Cell biology
- Biochemistry
- Molecular biology
Background:
- Cell wound repair necessitates rapid actin cytoskeleton remodeling.
- Actomyosin ring dynamics are critical for restoring cell cortex integrity during repair.
Purpose of the Study:
- To investigate the role of the Rab35-Mical-SelR pathway in regulating actomyosin ring dynamics during cell wound repair.
- To elucidate the mechanism of reversible actin redox in F-actin architecture and orientation.
Main Methods:
- Rab35 recruitment to cell wounds was assessed.
- Mical (actin-oxidizing enzyme) and SelR (reductase) recruitment and function were analyzed via knockdown experiments.
- Super-resolution microscopy was employed to examine F-actin architecture and orientation.
- Actin mutation at Methionine 44 was performed to assess its role.
Main Results:
- Rab35 is essential for actin ring assembly and disassembly at cell wounds.
- The Rab35-Mical-SelR pathway regulates actomyosin ring dynamics through reversible actin redox.
- Mical and SelR differentially impact F-actin architecture and orientation.
- A balanced redox cycle is required for proper actin ring formation and wound closure.
Conclusions:
- Reversible actin modifications dynamically regulate F-actin architecture and orientation.
- The Rab35-Mical-SelR pathway is a key regulator of actin ring assembly and disassembly for efficient cell wound repair.
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