ArticleBiophysical journal2016
Competition between Coiled-Coil Structures and the Impact on Myosin-10 Bundle Selection.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed.
- The filopodial myosin DdMyo7 is a slow, calcium-regulated motor.The Journal of biological chemistry · 2025Article
- De novo design of protein minibinder agonists of TLR3.Nature communications · 2025Article
- De novo design of protein minibinder agonists of TLR3.bioRxiv : the preprint server for biology · 2024Article
- Chiral growth of adherent filopodia.Biophysical journal · 2023Article
- The many roles of myosins in filopodia, microvilli and stereocilia.Current biology : CB · 2021Review
- Structural characterization of the self-association domain of swallow.Protein science : a publication of the Protein Society · 2021Article
- Optimized filopodia formation requires myosin tail domain cooperation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- The Antiparallel Dimerization of Myosin X Imparts Bundle Selectivity for Processive Motility.Biophysical journal · 2018Article
- Kinetic adaptation of human Myo19 for active mitochondrial transport to growing filopodia tips.Scientific reports · 2017Article
- Activated full-length myosin-X moves processively on filopodia with large steps toward diverse two-dimensional directions.Scientific reports · 2017Article
- A Combination of Diffusion and Active Translocation Localizes Myosin 10 to the Filopodial Tip.The Journal of biological chemistry · 2016Article
- The myosin X motor is optimized for movement on actin bundles.Nature communications · 2016Article
- Myosin Vc Is Specialized for Transport on a Secretory Superhighway.Current biology : CB · 2016Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Coiled-coil fusions are a useful approach to enforce dimerization in protein engineering. However, the final structures of coiled-coil fusion proteins have received relatively little attention. Here, we determine the structural outcome of adjacent parallel and antiparallel coiled coils. The targets are coiled coils that stabilize myosin-10 in single-molecule biophysical studies. We reveal the solution structure of a short, antiparallel, myosin-10 coiled-coil fused to the parallel GCN4-p1 coiled coil. Surprisingly, this structure is a continuous, antiparallel coiled coil where GCN4-p1 pairs with myosin-10 rather than itself. We also show that longer myosin-10 segments in these parallel/antiparallel fusions are dynamic and do not fold cooperatively. Our data resolve conflicting results on myosin-10 selection of actin filament bundles, demonstrating the importance of understanding coiled-coil orientation and stability.
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Registered trials
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