ArticleProceedings of the National Academy of Sciences of the United States of America2016
Myosin MyTH4-FERM structures highlight important principles of convergent evolution.
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, 26 citations in OpenAlex.
- The unconventional regulation of non-muscle myosins.Biophysical reviews · 2026Article
- Myosin 15 participates in assembly and remodeling of the presynapse.The Journal of cell biology · 2025Article
- FERM domain-containing proteins are active components of the cell nucleus.Life science alliance · 2024Review
- The dynamics of actin protrusions can be controlled by tip-localized myosin motors.The Journal of biological chemistry · 2024Article
- Comparative analysis of the MyTH4-FERM myosins reveals insights into the determinants of actin track selection in polarized epithelia.Molecular biology of the cell · 2021Article
- Article
- Propagation of F-actin disassembly via Myosin15-Mical interactions.Science advances · 2021Article
- A binding protein regulates myosin-7a dimerization and actin bundle assembly.Nature communications · 2021Article
- Novel MYO15A variants are associated with hearing loss in the two Iranian pedigrees.BMC medical genetics · 2020Article
- Optimized filopodia formation requires myosin tail domain cooperation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The first case of NSHL by direct impression onIranian journal of basic medical sciences · 2018Article
- 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
- Novel functions of CCM1 delimit the relationship of PTB/PH domains.Biochimica et biophysica acta. Proteins and proteomics · 2017Article
- Kinetic adaptation of human Myo19 for active mitochondrial transport to growing filopodia tips.Scientific reports · 2017Article
- ROS induced distribution of mitochondria to filopodia by Myo19 depends on a class specific tryptophan in the motor domain.Scientific reports · 2017Article
- Myosin 7 and its adaptors link cadherins to actin.Nature communications · 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
- MyTH4-FERM myosins in the assembly and maintenance of actin-based protrusions.Current opinion in cell biology · 2017Review
- MyTH4-FERM myosins have an ancient and conserved role in filopod formation.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
Myosins containing MyTH4-FERM (myosin tail homology 4-band 4.1, ezrin, radixin, moesin, or MF) domains in their tails are found in a wide range of phylogenetically divergent organisms, such as humans and the social amoeba Dictyostelium (Dd). Interestingly, evolutionarily distant MF myosins have similar roles in the extension of actin-filled membrane protrusions such as filopodia and bind to microtubules (MT), suggesting that the core functions of these MF myosins have been highly conserved over evolution. The structures of two DdMyo7 signature MF domains have been determined and comparison with mammalian MF structures reveals that characteristic features of MF domains are conserved. However, across millions of years of evolution conserved class-specific insertions are seen to alter the surfaces and the orientation of subdomains with respect to each other, likely resulting in new sites for binding partners. The MyTH4 domains of Myo10 and DdMyo7 bind to MT with micromolar affinity but, surprisingly, their MT binding sites are on opposite surfaces of the MyTH4 domain. The structural analysis in combination with comparison of diverse MF myosin sequences provides evidence that myosin tail domain features can be maintained without strict conservation of motifs. The results illustrate how tuning of existing features can give rise to new structures while preserving the general properties necessary for myosin tails. Thus, tinkering with the MF domain enables it to serve as a multifunctional platform for cooperative recruitment of various partners, allowing common properties such as autoinhibition of the motor and microtubule binding to arise through convergent evolution.
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