Membrane-bound myosin IC drives the chiral rotation of the gliding actin filament around its longitudinal axis

Myosin IC, a single-headed member of the myosin I family, specifically interacts with anionic phosphatidylinositol 4,5-bisphosphate (PI[4,5]P 2 ) 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 membran...

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Bibliographic Details
Published in:Scientific reports 2023-11, Vol.13 (1), p.19908-19908, Article 19908
Main Authors: Sato, Yusei, Yoshimura, Kohei, Matsuda, Kyohei, Haraguchi, Takeshi, Marumo, Akisato, Yamagishi, Masahiko, Sato, Suguru, Ito, Kohji, Yajima, Junichiro
Format: Article
Language:English
Subjects:
631/57/343
631/80/128
Actin
Cell membranes
Chirality
Cytoskeleton
Filaments
Gliding
Handedness
Homology
Humanities and Social Sciences
Membranes
multidisciplinary
Myosin
Phosphatidylinositol 4,5-diphosphate
Phospholipid composition
Phospholipids
Pleckstrin
Quantum dots
Science
Science (multidisciplinary)
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Summary:Myosin IC, a single-headed member of the myosin I family, specifically interacts with anionic phosphatidylinositol 4,5-bisphosphate (PI[4,5]P 2 ) 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 2 concentrations revealed that the rotational pitch was longer at lower PI(4,5)P 2 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.
ISSN:2045-2322
2045-2322
DOI:10.1038/s41598-023-47125-5