AI Article Synopsis
- * This study tracked the movement of actin filaments using quantum dots to show that myosin IC can cause the filaments to rotate as they glide across a surface coated with myosin IC.
- * The research found that the degree of rotation is influenced by the concentration of a specific phospholipid (PI[4,5]P) in the membrane, suggesting that the mechanical actions of myosin IC can be adjusted depending on the lipid environment.
Article Abstract
Myosin IC, a single-headed member of the myosin I family, specifically interacts with anionic phosphatidylinositol 4,5-bisphosphate (PI[4,5]P) in the cell membrane via the pleckstrin homology domain located in the myosin IC tail. Myosin IC is widely expressed and physically links the cell membrane to the actin cytoskeleton; it plays various roles in membrane-associated physiological processes, including establishing cellular chirality, lipid transportation, and mechanosensing. In this study, we evaluated the motility of full-length myosin IC of Drosophila melanogaster via the three-dimensional tracking of quantum dots bound to actin filaments that glided over a membrane-bound myosin IC-coated surface. The results revealed that myosin IC drove a left-handed rotational motion in the gliding actin filament around its longitudinal axis, indicating that myosin IC generated a torque perpendicular to the gliding direction of the actin filament. The quantification of the rotational motion of actin filaments on fluid membranes containing different PI(4,5)P concentrations revealed that the rotational pitch was longer at lower PI(4,5)P concentrations. These results suggest that the torque generated by membrane-bound myosin IC molecules can be modulated based on the phospholipid composition of the cell membrane.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10646037 | PMC |
| http://dx.doi.org/10.1038/s41598-023-47125-5 | DOI Listing |
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