ArticleProceedings of the National Academy of Sciences of the United States of America2011
Structure and function of the interacting domains of Spire and Fmn-family formins.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 96 citations in OpenAlex.
- Article
- The Influence of Drosophila Spire and Myosin V During Mid-Oogenesis Is Independent of Their Direct Interaction.Cytoskeleton (Hoboken, N.J.) · 2026Article
- The Cappuccino interactome reveals an intracellular role for Semaphorin-2a inbioRxiv : the preprint server for biology · 2026Article
- Nascent dendrite branches initiated by a localized burst of Spire-dependent actin polymerization.Development (Cambridge, England) · 2025Article
- Disulfidptosis: a novel cell death modality induced by actin cytoskeleton collapse and a promising target for cancer therapeutics.Cell communication and signaling : CCS · 2024Review
- Identification of structural variation related to spawn capability of Penaeus vannamei.BMC genomics · 2024Article
- Nuclear F-actin assembly on damaged chromatin is regulated by DYRK1A and Spir1 phosphorylation.Nucleic acids research · 2024Article
- Actomyosin organelle functions of SPIRE actin nucleators precede animal evolution.Communications biology · 2024Article
- Discovery of Inhibitory Fragments That Selectively Target Spire2-FMN2 Interaction.Journal of medicinal chemistry · 2023Article
- Antagonistic Activities of Fmn2 and ADF Regulate Axonal F-Actin Patch Dynamics and the Initiation of Collateral Branching.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- Dual control of formin-nucleated actin assembly by the chromatin and ER in mouse oocytes.Current biology : CB · 2022Article
- Heterozygous FMN2 missense variant found in a family case of premature ovarian insufficiency.Journal of ovarian research · 2022Article
- The actin nucleator Spir-1 is a virus restriction factor that promotes innate immune signalling.PLoS pathogens · 2022Article
- A teamwork promotion of formin-mediated actin nucleation by Bud6 and Aip5 inMolecular biology of the cell · 2022Article
- Insight into membraneless organelles and their associated proteins: Drivers, Clients and Regulators.Computational and structural biotechnology journal · 2021Article
- Rab27a co-ordinates actin-dependent transport by controlling organelle-associated motors and track assembly proteins.Nature communications · 2020Article
- Competition for delivery of profilin-actin to barbed ends limits the rate of formin-mediated actin filament elongation.The Journal of biological chemistry · 2020Article
- Spire stimulates nucleation by Cappuccino and binds both ends of actin filaments.Molecular biology of the cell · 2020Article
- Understanding brain development - Indian researchers' past, present and growing contribution.The International journal of developmental biology · 2020Review
- Exploring the iceberg: Prospects of coordinated myosin V and actin assembly functions in transport processes.Small GTPases · 2019Review
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Authors and funding
8 authors at 4 institutions in 1 country.
Funding
Abstract
Evidence for cooperation between actin nucleators is growing. The WH2-containing nucleator Spire and the formin Cappuccino interact directly, and both are essential for assembly of an actin mesh during Drosophila oogenesis. Their interaction requires the kinase noncatalytic C-lobe domain (KIND) domain of Spire and the C-terminal tail of the formin. Here we describe the crystal structure of the KIND domain of human Spir1 alone and in complex with the tail of Fmn2, a mammalian ortholog of Cappuccino. The KIND domain is structurally similar to the C-lobe of protein kinases. The Fmn2 tail is coordinated in an acidic cleft at the base of the domain that appears to have evolved via deletion of a helix from the canonical kinase fold. Our functional analysis of Cappuccino reveals an unexpected requirement for its tail in actin assembly. In addition, we find that the KIND/tail interaction blocks nucleation by Cappuccino and promotes its displacement from filament barbed ends providing insight into possible modes of cooperation between Spire and Cappuccino.
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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.