ArticlemicroPublication biology2026
Exploring phosphoregulation of MYO3A using quantitative fluorescence image analysis in COS7 cells.
Article in microPublication biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
1 citing paper in PubMed.
- Exploring phosphoregulation of MYO3A using quantitative fluorescence image analysis in COS7 cells.microPublication biology · 2026Article
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Authors and funding
2 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Myosin IIIA is an unconventional myosin that contains a kinase domain, and is involved in the formation of hair-cell stereocilia. To investigate its regulatory roles, we mimicked phosphorylation in mchr-MYO3AΔK constructs and assayed their ability to influence filopodial properties in COS7 cells. The phosphomimics generated fewer filopodia. Coexpression of mchr-MYO3AΔK with a GFP-construct containing only the MYO3A kinase domain also resulted in generation of fewer filopodia. Structural predictions suggest that the phosphorylation sites inhibit actin/MYO3A interactions. Taken together, these analyses link MYO3A phosphorylation with the regulation of its ability to create actin protrusions such as filopodia and stereocilia.
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Registered trials
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