ArticleStructure (London, England : 1993)2015
Structure of a Bud6/Actin Complex Reveals a Novel WH2-like Actin Monomer Recruitment Motif.
Article in Structure (London, England : 1993), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 18 citations in OpenAlex.
- Aip5 forms a "composite" actin nucleator with Bud6 and caps pointed ends of actin filaments.The Journal of cell biology · 2025Article
- The roles of yeast formins and their regulators Bud6 and Bil2 in the pheromone response.Molecular biology of the cell · 2024Article
- Review
- Spire stimulates nucleation by Cappuccino and binds both ends of actin filaments.Molecular biology of the cell · 2020Article
- YFR016c/Aip5 is part of an actin nucleation complex in yeast.Biology open · 2019Article
- Non-catalytic signaling by pseudokinase ILK for regulating cell adhesion.Nature communications · 2018Article
- Integrated control of formin-mediated actin assembly by a stationary inhibitor and a mobile activator.The Journal of cell biology · 2018Article
- Crystal Structure of Leiomodin 2 in Complex with Actin: A Structural and Functional Reexamination.Biophysical journal · 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
Corrections and comments
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
In budding yeast, the actin-binding protein Bud6 cooperates with formins Bni1 and Bnr1 to catalyze the assembly of actin filaments. The nucleation-enhancing activity of Bud6 requires both a "core" domain that binds to the formin and a "flank" domain that binds monomeric actin. Here, we describe the structure of the Bud6 flank domain in complex with actin. Two helices in Bud6(flank) interact with actin; one binds in a groove at the barbed end of the actin monomer in a manner closely resembling the helix of WH2 domains, a motif found in many actin nucleation factors. The second helix rises along the face of actin. Mutational analysis verifies the importance of these Bud6-actin contacts for nucleation-enhancing activity. The Bud6 binding site on actin overlaps with that of the formin FH2 domain and is also incompatible with inter-subunit contacts in F-actin, suggesting that Bud6 interacts only transiently with actin monomers during filament nucleation.
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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.