A method for reconstituting the motility of membrane-bound myosin on the surface of the cell-sized W/O droplet.
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| Main Authors: | , , , , |
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| Format: | Artículo científico |
| Language: | en |
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MethodsX
2026
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| _version_ | 1868266102690152448 |
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| author | Sato, Yusei Sumiyoshi, Rieko Hayashi, Masahito Yamagishi, Masahiko Yajima, Junichiro |
| author_facet | Sato, Yusei Sumiyoshi, Rieko Hayashi, Masahito Yamagishi, Masahiko Yajima, Junichiro Sato, Yusei Sumiyoshi, Rieko Hayashi, Masahito Yamagishi, Masahiko Yajima, Junichiro |
| collection | PubMed - marine biology |
| contents | A method for reconstituting the motility of membrane-bound myosin on the surface of the cell-sized W/O droplet. Sato, Yusei Sumiyoshi, Rieko Hayashi, Masahito Yamagishi, Masahiko Yajima, Junichiro Membrane-bound myosin generates force through interactions with the cytoskeletal actin filament beneath the cell membrane and constitutes the mechanical basis for living cells. Myosin ID, a membrane-bound myosin, drives the gliding motion of actin filaments and binds to phospholipids in the lipid membrane of a living cell. Here, we describe the actin filament gliding assay, a method that reconstitutes the motility of actomyosin that dynamically interacts with lipid membranes within water-in-oil (W/O) droplets, which mimic the confined geometry of the intracellular environment. Our method enables quantification of the gliding velocity of actin filaments driven by myosin ID on the inner surface of W/O droplets surrounded by a phospholipid membrane. The actin filament gliding assay provides a valuable platform for reconstituting the motile properties of other membrane-bound myosins on membrane surfaces in confined spaces and for analyzing the dynamics of actomyosin networks. The main features and applications of this method are as follows:•Reconstitution of actin filament gliding driven by membrane-bound myosin ID within confined water-in-oil droplets.•Quantitative evaluation of actomyosin dynamics on the inner surface of the lipid membrane within water-in-oil-droplets.•Broadly applicable assay platform for studying the motile properties of membrane-associated myosin families. |
| format | Artículo científico |
| id | pubmed_41503092 |
| institution | PubMed |
| language | en |
| publishDate | 2026 |
| publisher | MethodsX |
| record_format | pubmed |
| spellingShingle | A method for reconstituting the motility of membrane-bound myosin on the surface of the cell-sized W/O droplet. Sato, Yusei Sumiyoshi, Rieko Hayashi, Masahito Yamagishi, Masahiko Yajima, Junichiro A method for reconstituting the motility of membrane-bound myosin on the surface of the cell-sized W/O droplet. Sato, Yusei Sumiyoshi, Rieko Hayashi, Masahito Yamagishi, Masahiko Yajima, Junichiro Membrane-bound myosin generates force through interactions with the cytoskeletal actin filament beneath the cell membrane and constitutes the mechanical basis for living cells. Myosin ID, a membrane-bound myosin, drives the gliding motion of actin filaments and binds to phospholipids in the lipid membrane of a living cell. Here, we describe the actin filament gliding assay, a method that reconstitutes the motility of actomyosin that dynamically interacts with lipid membranes within water-in-oil (W/O) droplets, which mimic the confined geometry of the intracellular environment. Our method enables quantification of the gliding velocity of actin filaments driven by myosin ID on the inner surface of W/O droplets surrounded by a phospholipid membrane. The actin filament gliding assay provides a valuable platform for reconstituting the motile properties of other membrane-bound myosins on membrane surfaces in confined spaces and for analyzing the dynamics of actomyosin networks. The main features and applications of this method are as follows:•Reconstitution of actin filament gliding driven by membrane-bound myosin ID within confined water-in-oil droplets.•Quantitative evaluation of actomyosin dynamics on the inner surface of the lipid membrane within water-in-oil-droplets.•Broadly applicable assay platform for studying the motile properties of membrane-associated myosin families. |
| title | A method for reconstituting the motility of membrane-bound myosin on the surface of the cell-sized W/O droplet. |
| url | https://pubmed.ncbi.nlm.nih.gov/41503092/ |