ArticleACS applied materials & interfaces2017
Parallel Compression Is a Fast Low-Cost Assay for the High-Throughput Screening of Mechanosensory Cytoskeletal Proteins in Cells.
Article in ACS applied materials & interfaces, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 6 citations in OpenAlex.
- A continuum model of mechanosensation based on contractility kit assembly.Biophysical journal · 2025Article
- Discovery and Quantitative Dissection of Cytokinesis Mechanisms Using Dictyostelium discoideum.Methods in molecular biology (Clifton, N.J.) · 2024Article
- The lectin Discoidin I acts in the cytoplasm to help assemble the contractile machinery.The Journal of cell biology · 2022Article
- Cell-in-cell structure mediates in-cell killing suppressed by CD44.Cell discovery · 2022Article
- PCDH7 Inhibits the Formation of Homotypic Cell-in-Cell Structure.Frontiers in cell and developmental biology · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Cellular mechanosensing is critical for many biological processes, including cell differentiation, proliferation, migration, and tissue morphogenesis. The actin cytoskeletal proteins play important roles in cellular mechanosensing. Many techniques have been used to investigate the mechanosensory behaviors of these proteins. However, a fast, low-cost assay for the quantitative characterization of these proteins is still lacking. Here, we demonstrate that compression assay using agarose overlay is suitable for the high throughput screening of mechanosensory proteins in live cells while requiring minimal experimental setup. We used several well-studied myosin II mutants to assess the compression assay. On the basis of elasticity theories, we simulated the mechanosensory accumulation of myosin II's and quantitatively reproduced the experimentally observed protein dynamics. Combining the compression assay with confocal microscopy, we monitored the polarization of myosin II oligomers at the subcellular level. The polarization was dependent on the ratio of the two principal strains of the cellular deformations. Finally, we demonstrated that this technique could be used on the investigation of other mechanosensory proteins.
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Registered trials
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