ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structure of the formin-interaction domain of the actin nucleation-promoting factor Bud6.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 34 citations in OpenAlex.
- The roles of yeast formins and their regulators Bud6 and Bil2 in the pheromone response.Molecular biology of the cell · 2024Article
- A teamwork promotion of formin-mediated actin nucleation by Bud6 and Aip5 inMolecular biology of the cell · 2022Article
- Type V myosin focuses the polarisome and shapes the tip of yeast cells.The Journal of cell biology · 2021Article
- Orchestrated actin nucleation by theThe Journal of biological chemistry · 2020Article
- A time-resolved interaction analysis of Bem1 reconstructs the flow of Cdc42 during polar growth.Life science alliance · 2020Article
- Spire stimulates nucleation by Cappuccino and binds both ends of actin filaments.Molecular biology of the cell · 2020Article
- Polarisome scaffolder Spa2-mediated macromolecular condensation of Aip5 for actin polymerization.Nature communications · 2019Article
- Neuronal drebrin A directly interacts with mDia2 formin to inhibit actin assembly.Molecular biology of the cell · 2019Article
- Integrated control of formin-mediated actin assembly by a stationary inhibitor and a mobile activator.The Journal of cell biology · 2018Article
- Role of Mitochondrial Retrograde Pathway in Regulating Ethanol-Inducible Filamentous Growth in Yeast.Frontiers in physiology · 2017Article
- The WH2 Domain and Actin Nucleation: Necessary but Insufficient.Trends in biochemical sciences · 2016Review
- Role of the C-terminal Extension of Formin 2 in Its Activation by Spire Protein and Processive Assembly of Actin Filaments.The Journal of biological chemistry · 2016Article
- Structure of a Bud6/Actin Complex Reveals a Novel WH2-like Actin Monomer Recruitment Motif.Structure (London, England : 1993) · 2015Article
- The Carboxy-Terminal Tails of Septins Cdc11 and Shs1 Recruit Myosin-II Binding Factor Bni5 to the Bud Neck in Saccharomyces cerevisiae.Genetics · 2015Article
- The role of formin tails in actin nucleation, processive elongation, and filament bundling.The Journal of biological chemistry · 2014Article
- The long and viscous road: uncovering nuclear diffusion barriers in closed mitosis.PLoS computational biology · 2014Article
- Direct interaction between two actin nucleators is required in Drosophila oogenesis.Development (Cambridge, England) · 2013Article
- Rickettsia Sca2 has evolved formin-like activity through a different molecular mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Ligand-induced activation of a formin-NPF pair leads to collaborative actin nucleation.The Journal of cell biology · 2013Article
- Drosophila homologues of adenomatous polyposis coli (APC) and the formin diaphanous collaborate by a conserved mechanism to stimulate actin filament assembly.The Journal of biological chemistry · 2013Article
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Formin proteins and their associated factors cooperate to assemble unbranched actin filaments in diverse cellular structures. The Saccharomyces cerevisiae formin Bni1 and its associated nucleation-promoting factor (NPF) Bud6 generate actin cables and mediate polarized cell growth. Bud6 binds to both the tail of the formin and G-actin, thereby recruiting monomeric actin to the formin to create a nucleation seed. Here, we structurally and functionally dissect the nucleation-promoting C-terminal region of Bud6 into a Bni1-binding "core" domain and a G-actin binding "flank" domain. The ∼2-Å resolution crystal structure of the Bud6 core domain reveals an elongated dimeric rod with a unique fold resembling a triple-helical coiled-coil. Binding and actin-assembly assays show that conserved residues on the surface of this domain mediate binding to Bni1 and are required for NPF activity. We find that the Bni1 dimer binds two Bud6 dimers and that the Bud6 flank binds a single G-actin molecule. These findings suggest a model in which a Bni1/Bud6 complex with a 2:4 subunit stoichiometry assembles a nucleation seed with Bud6 coordinating up to four actin subunits.
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