ArticleMolecular biology of the cell2016
Common formin-regulating sequences in Smy1 and Bud14 are required for the control of actin cable assembly in vivo.
Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 31 citations in OpenAlex.
- Distinct disassembly modes shape cytoskeletal assembly and fluctuations.Biophysical reports · 2026Article
- Functional redundancy and formin-isoform independent localization of tropomyosin paralogs in Saccharomyces cerevisiae.PLoS genetics · 2025Article
- Quantitative Signatures of Disassembly Mechanisms Modulating Filament and Bundle Assembly in a Shared Pool.bioRxiv : the preprint server for biology · 2025Article
- Sequential recruitment of F-BAR proteins controls cytoskeletal crosstalk at the yeast bud neck.Current biology : CB · 2025Article
- Improved tools for live imaging of F-actin structures in yeast.Molecular biology of the cell · 2024Article
- Length control emerges from cytoskeletal network geometry.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The roles of yeast formins and their regulators Bud6 and Bil2 in the pheromone response.Molecular biology of the cell · 2024Article
- Cytosolic concentrations of actin binding proteins and the implications for in vivo F-actin turnover.The Journal of cell biology · 2023Article
- Length control emerges from cytoskeletal network geometry.bioRxiv : the preprint server for biology · 2023Article
- Quantitative Analysis of Actin Cable Length in Yeast.Bio-protocol · 2022Article
- Enhancing biofuels production by engineering the actin cytoskeleton in Saccharomyces cerevisiae.Nature communications · 2022Article
- How to assemble a scale-invariant gradient.eLife · 2022Article
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- Bil2 Is a Novel Inhibitor of the Yeast Formin Bnr1 Required for Proper Actin Cable Organization and Polarized Secretion.Frontiers in cell and developmental biology · 2021Article
- A septin-Hof1 scaffold at the yeast bud neck binds and organizes actin cables.Molecular biology of the cell · 2020Article
- Genetically inspired in vitro reconstitution ofMolecular biology of the cell · 2020Article
- Structural mechanism for versatile cargo recognition by the yeast class V myosin Myo2.The Journal of biological chemistry · 2019Article
- Integrated control of formin-mediated actin assembly by a stationary inhibitor and a mobile activator.The Journal of cell biology · 2018Article
- Control of Formin Distribution and Actin Cable Assembly by the E3 Ubiquitin Ligases Dma1 and Dma2.Genetics · 2016Article
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5 authors at 1 institution in 1 country.
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Abstract
Formins comprise a large family of proteins with diverse roles in remodeling the actin cytoskeleton. However, the spatiotemporal mechanisms used by cells to control formin activities are only beginning to be understood. Here we dissected Smy1, which has dual roles in regulating formins and myosin. Using mutagenesis, we identified specific sequences in Smy1 critical for its in vitro inhibitory effects on the FH2 domain of the formin Bnr1. By integrating smy1 alleles targeting those sequences, we genetically uncoupled Smy1's functions in regulating formins and myosin. Quantitative imaging analysis further demonstrated that the ability of Smy1 to directly control Bnr1 activity is crucial in vivo for proper actin cable length, shape, and velocity and, in turn, efficient secretory vesicle transport. A Smy1-like sequence motif was also identified in a different Bnr1 regulator, Bud14, and found to be essential for Bud14 functions in regulating actin cable architecture and function in vivo. Together these observations reveal unanticipated mechanistic ties between two distinct formin regulators. Further, they emphasize the importance of tightly controlling formin activities in vivo to generate specialized geometries and dynamics of actin structures tailored to their physiological roles.
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