ArticleDevelopmental cell2009
Displacement of formins from growing barbed ends by bud14 is critical for actin cable architecture and function.
Article in Developmental cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
50 citing papers in PubMed, 76 citations in OpenAlex.
- Functional redundancy and formin-isoform independent localization of tropomyosin paralogs in Saccharomyces cerevisiae.PLoS genetics · 2025Article
- Sequential recruitment of F-BAR proteins controls cytoskeletal crosstalk at the yeast bud neck.Current biology : CB · 2025Article
- The mode of subunit addition regulates the processive elongation of actin filaments by formin.The Journal of biological chemistry · 2025Article
- Length control emerges from cytoskeletal network geometry.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Length control emerges from cytoskeletal network geometry.bioRxiv : the preprint server for biology · 2023Article
- Multicomponent regulation of actin barbed end assembly by twinfilin, formin and capping protein.Nature communications · 2023Article
- Multicomponent regulation of actin barbed end assembly by twinfilin, formin and capping protein.bioRxiv : the preprint server for biology · 2023Article
- mNG-tagged fusion proteins and nanobodies to visualize tropomyosins in yeast and mammalian cells.Journal of cell science · 2022Article
- Article
- Designer membraneless organelles sequester native factors for control of cell behavior.Nature chemical biology · 2021Article
- 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
- 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
- Article
- Control of Formin Distribution and Actin Cable Assembly by the E3 Ubiquitin Ligases Dma1 and Dma2.Genetics · 2016Article
- The final cut: cell polarity meets cytokinesis at the bud neck in S. cerevisiae.Cellular and molecular life sciences : CMLS · 2016Review
- Design Principles of Length Control of Cytoskeletal Structures.Annual review of biophysics · 2016Review
- Accelerated actin filament polymerization from microtubule plus ends.Science (New York, N.Y.) · 2016Article
- Common formin-regulating sequences in Smy1 and Bud14 are required for the control of actin cable assembly in vivo.Molecular biology of the cell · 2016Article
- Requirement of Phosphoinositides Containing Stearic Acid To Control Cell Polarity.Molecular and cellular biology · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Normal cellular development and function require tight spatiotemporal control of actin assembly. Formins are potent actin assembly factors that protect the growing ends of actin filaments from capping proteins. However, it is unresolved how the duration of formin-mediated actin assembly events is controlled, whether formins are actively displaced from growing ends, and how filament length is regulated in vivo. Here, we identify Bud14 as a high-affinity inhibitor of the yeast formin Bnr1 that rapidly displaces the Bnr1 FH2 domain from growing barbed ends. Consistent with these activities, bud14Delta cells display fewer actin cables, which are aberrantly long, bent, and latrunculinA resistant, leading to defects in secretory vesicle movement. Moreover, bud14Delta suppressed mutations that cause abnormally numerous and shortened cables, restoring wild-type actin architecture. From these results, we propose that formin displacement factors regulate filament length and are required in vivo to maintain proper actin network architecture and 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.