ArticleProceedings of the National Academy of Sciences of the United States of America2016
MyTH4-FERM myosins have an ancient and conserved role in filopod formation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 43 citations in OpenAlex.
- Modulation of Filopodial Myosin Function.bioRxiv : the preprint server for biology · 2025Article
- Filopodia numbers impact chemotactic migration speed.bioRxiv : the preprint server for biology · 2025Article
- The filopodial myosin DdMyo7 is a slow, calcium-regulated motor.The Journal of biological chemistry · 2025Article
- Hundreds of myosin 10s are pushed to the tips of filopodia and could cause traffic jams on actin.eLife · 2024Article
- Hundreds of myosin 10s are pushed to the tips of filopodia and could cause traffic jams on actin.bioRxiv : the preprint server for biology · 2024Article
- filoVision - using deep learning and tip markers to automate filopodia analysis.Journal of cell science · 2024Article
- Myosin XV is a negative regulator of signaling filopodia during long-range lateral inhibition.Developmental biology · 2024Article
- Protrusion growth driven by myosin-generated force.Developmental cell · 2023Article
- Adhesion ofFrontiers in cell and developmental biology · 2022Review
- Article
- The many roles of myosins in filopodia, microvilli and stereocilia.Current biology : CB · 2021Review
- The actin networks of chytrid fungi reveal evolutionary loss of cytoskeletal complexity in the fungal kingdom.Current biology : CB · 2021Article
- A binding protein regulates myosin-7a dimerization and actin bundle assembly.Nature communications · 2021Article
- Optimized filopodia formation requires myosin tail domain cooperation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Filopodia and focal adhesions: An integrated system driving branching morphogenesis in neuronal pathfinding and angiogenesis.Developmental biology · 2019Review
- Brush border protocadherin CDHR2 promotes the elongation and maximized packing of microvilli in vivo.Molecular biology of the cell · 2019Article
- Myosin-X knockout is semi-lethal and demonstrates that myosin-X functions in neural tube closure, pigmentation, hyaloid vasculature regression, and filopodia formation.Scientific reports · 2017Article
- Structure of Myo7b/USH1C complex suggests a general PDZ domain binding mode by MyTH4-FERM myosins.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Activated full-length myosin-X moves processively on filopodia with large steps toward diverse two-dimensional directions.Scientific reports · 2017Article
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
The formation of filopodia in Metazoa and Amoebozoa requires the activity of myosin 10 (Myo10) in mammalian cells and of Dictyostelium unconventional myosin 7 (DdMyo7) in the social amoeba Dictyostelium However, the exact roles of these MyTH4-FERM myosins (myosin tail homology 4-band 4.1, ezrin, radixin, moesin; MF) in the initiation and elongation of filopodia are not well defined and may reflect conserved functions among phylogenetically diverse MF myosins. Phylogenetic analysis of MF myosin domains suggests that a single ancestral MF myosin existed with a structure similar to DdMyo7, which has two MF domains, and that subsequent duplications in the metazoan lineage produced its functional homolog Myo10. The essential functional features of the DdMyo7 myosin were identified using quantitative live-cell imaging to characterize the ability of various mutants to rescue filopod formation in myo7-null cells. The two MF domains were found to function redundantly in filopod formation with the C-terminal FERM domain regulating both the number of filopodia and their elongation velocity. DdMyo7 mutants consisting solely of the motor plus a single MyTH4 domain were found to be capable of rescuing the formation of filopodia, establishing the minimal elements necessary for the function of this myosin. Interestingly, a chimeric myosin with the Myo10 MF domain fused to the DdMyo7 motor also was capable of rescuing filopod formation in the myo7-null mutant, supporting fundamental functional conservation between these two distant myosins. Together, these findings reveal that MF myosins have an ancient and conserved role in filopod formation.
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