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Cell Biology: Capturing Formin's Mechano-Inhibition
Dimitrios Vavylonis1, Brandon G Horan1
1Department of Physics, Lehigh University, Bethlehem, PA 18015, USA.
Current Biology : CB
|October 11, 2017
Summary
Formins build actin structures for cell division. A new study reveals myosin pulling inhibits formin actin polymerization, impacting cellular force sensing mechanisms.
Area of Science:
- Cell Biology
- Biophysics
Background:
- Formins are essential proteins that regulate actin cytoskeleton dynamics.
- Actin polymerization by formins is crucial for cytokinesis, the process of cell division.
- Contractile ring formation involves formins and myosin motors.
Purpose of the Study:
- To investigate the interplay between formin-mediated actin polymerization and myosin activity in vitro.
- To understand how mechanical forces exerted by myosin affect actin filament assembly.
Main Methods:
- In vitro reconstitution of fission yeast contractile ring precursor nodes.
- Utilizing purified formins and myosin.
- Observing actin filament polymerization dynamics under mechanical tension.
Main Results:
- Formin-mediated actin polymerization is significantly inhibited when myosin captures and pulls actin filaments.
- Myosin's mechanical activity directly interferes with the polymerization process mediated by formins.
Conclusions:
- Myosin-driven forces actively regulate formin-dependent actin polymerization.
- This interaction has broad implications for understanding cellular mechanosensing and the mechanics of cytokinesis.
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