ArticleProceedings of the National Academy of Sciences of the United States of America2011
Cargo binding activates myosin VIIA motor function in cells.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 73 citations in OpenAlex.
- Tonotopic specialization of MYO7A isoforms in auditory hair cells.Nature communications · 2026Article
- HomozygousTranslational andrology and urology · 2026Article
- Single-molecule fluorescence microscopy reveals regulatory mechanisms of MYO7A-driven cargo transport in stereocilia of live inner ear hair cells.Nature communications · 2025Article
- The filopodial myosin DdMyo7 is a slow, calcium-regulated motor.The Journal of biological chemistry · 2025Article
- Select autosomal dominant DFNA11 deafness variants activate Myo7A targeting in epithelial cells.Journal of cell science · 2025Article
- Myosin-based nucleation of actin filaments contributes to stereocilia development critical for hearing.Nature communications · 2025Article
- Pathophysiology of human hearing loss associated with variants in myosins.Frontiers in physiology · 2024Review
- Myosin motors in sensory hair bundle assembly.Current opinion in cell biology · 2022Review
- Selective binding and transport of protocadherin 15 isoforms by stereocilia unconventional myosins in a heterologous expression system.Scientific reports · 2022Article
- The role of motor proteins in photoreceptor protein transport and visual function.Ophthalmic genetics · 2022Article
- Mitochondria-associated myosin 19 processively transports mitochondria on actin tracks in living cells.The Journal of biological chemistry · 2022Article
- 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
- The many roles of myosins in filopodia, microvilli and stereocilia.Current biology : CB · 2021Review
- A binding protein regulates myosin-7a dimerization and actin bundle assembly.Nature communications · 2021Article
- Functional Role of Class III Myosins in Hair Cells.Frontiers in cell and developmental biology · 2021Review
- Nonmuscle myosin-2 contractility-dependent actin turnover limits the length of epithelial microvilli.Molecular biology of the cell · 2020Article
- Unconventional Myosins: How Regulation Meets Function.International journal of molecular sciences · 2019Review
- Optimized filopodia formation requires myosin tail domain cooperation.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- F5-Peptide and mTORC1/rpS6 Effectively Enhance BTB Transport Function in the Testis-Lesson From the Adjudin Model.Endocrinology · 2019Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Myosin VIIA, thought to be involved in human auditory function, is a gene responsible for human Usher syndrome type 1B, which causes hearing and visual loss. Recent studies have suggested that it can move processively if it forms a dimer. Nevertheless, it exists as a monomer in vitro, unlike the well-known two-headed processive myosin Va. Here we studied the molecular mechanism, which is currently unknown, of activating myosin VIIA as a cargo-transporting motor. Human myosin VIIA was present throughout cytosol, but it moved to the tip of filopodia upon the formation of dimer induced by dimer-inducing reagent. The forced dimer of myosin VIIA translocated its cargo molecule, MyRip, to the tip of filopodia, whereas myosin VIIA without the forced dimer-forming module does not translocate to the filopodial tips. These results suggest that dimer formation of myosin VIIA is important for its cargo-transporting activity. On the other hand, myosin VIIA without the forced dimerization module became translocated to the filopodial tips in the presence of cargo complex, i.e., MyRip/Rab27a, and transported its cargo complex to the tip. Coexpression of MyRip promoted the association of myosin VIIA to vesicles and the dimer formation. These results suggest that association of myosin VIIA monomers with membrane via the MyRip/Rab27a complex facilitates the cargo-transporting activity of myosin VIIA, which is achieved by cluster formation on the membrane, where it possibly forms a dimer. Present findings support that MyRip, a cargo molecule, functions as an activator of myosin VIIA transporter function.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.