ArticleProceedings of the National Academy of Sciences of the United States of America2009
A FERM domain autoregulates Drosophila myosin 7a activity.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
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Who cites it
65 citing papers in PubMed.
- Single-molecule fluorescence microscopy reveals regulatory mechanisms of MYO7A-driven cargo transport in stereocilia of live inner ear hair cells.Nature communications · 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
- The actomyosin system is essential for the integrity of the endosomal system in bloodstream formeLife · 2024Article
- MultiBac System-based Purification and Biophysical Characterization of Human Myosin-7a.Journal of visualized experiments : JoVE · 2024Article
- Autoinhibition and activation of myosin VI revealed by its cryo-EM structure.Nature communications · 2024Article
- Autoinhibition and activation mechanisms revealed by the triangular-shaped structure of myosin Va.Science advances · 2022Article
- On the association between Chiari malformation type 1, bone mineral density and bone related genes.Bone reports · 2022Article
- The role of motor proteins in photoreceptor protein transport and visual function.Ophthalmic genetics · 2022Article
- Clinical Heterogeneity Associated withBiomedicines · 2022Article
- Deafness mutation in the MYO3A motor domain impairs actin protrusion elongation mechanism.Molecular biology of the cell · 2022Article
- Purification of Cytoskeletal Proteins by Fast Protein Liquid Chromatography (FPLC) Using an ÄKTA Start System.Methods in molecular biology (Clifton, N.J.) · 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
- The C-terminal tail extension of myosin 16 acts as a molten globule, including intrinsically disordered regions, and interacts with the N-terminal ankyrin.The Journal of biological chemistry · 2021Article
- Article
- The formin inhibitor SMIFH2 inhibits members of the myosin superfamily.Journal of cell science · 2021Article
- Spectrum ofGenes · 2021Article
- Mutations in Drosophila crinkled/Myosin VIIA disrupt denticle morphogenesis.Developmental biology · 2021Article
- A binding protein regulates myosin-7a dimerization and actin bundle assembly.Nature communications · 2021Article
- ER/K-link-Leveraging a native protein linker to probe dynamic cellular interactions.Methods in enzymology · 2021Review
5 more citing papers are in PubMed but not listed here.
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8 authors.
Funding
Abstract
Full-length Drosophila myosin 7a (myosin 7a-FL) has a complex tail containing a short predicted coiled coil followed by a MyTH4-FERM domain, an SH3 domain, and a C-terminal MyTH4-FERM domain. Myosin 7a-FL expressed in Sf9 cells is monomeric despite the predicted coiled coil. We showed previously that Subfragment-1 (S1) from this myosin has MgATPase of V(max) approximately 1 s(-1) and K(ATPase) approximately 1 microM actin. We find that myosin 7a-FL has V(max) similar to S1 but K(ATPase) approximately 30 microM. Thus, at low actin concentrations (5 microM), the MgATPase of S1 is fully activated, whereas that of myosin 7a-FL is low, suggesting that the tail regulates activity. Electron microscopy of myosin 7a-FL with ATP shows the tail is tightly bent back against the motor domain. Myosin 7a-FL extends at either high ionic strength or without ATP, revealing the motor domain, lever, and tail. A series of C-terminal truncations show that deletion of 99 aa (the MyTH7 subdomain of the C-terminal FERM domain) is sufficient to abolish bending, and the K(ATPase) is then similar to S1. This region is highly conserved in myosin 7a. We found that a double mutation in it, R2140A-K2143A, abolishes bending and reduces K(ATPase) to S1 levels. In addition, the expressed C-terminal FERM domain binds actin with K(d) approximately 30 microM regardless of ATP, similar to the K(ATPase) value for myosin 7a-FL. We propose that at low cellular actin concentrations, myosin 7a-FL is bent and inactive, but at high actin concentrations, it is unfolded and active because the C-terminal FERM domain binds to actin.
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