ArticleMolecular biology of the cell2020
Spire stimulates nucleation by Cappuccino and binds both ends of actin filaments.
Article in Molecular biology of the cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- Article
- The Cappuccino interactome reveals an intracellular role for Semaphorin-2a inbioRxiv : the preprint server for biology · 2026Article
- Aip5 forms a "composite" actin nucleator with Bud6 and caps pointed ends of actin filaments.The Journal of cell biology · 2025Article
- The mode of subunit addition regulates the processive elongation of actin filaments by formin.The Journal of biological chemistry · 2025Article
- Actin filament dynamics at barbed ends: New structures, new insights.Current opinion in cell biology · 2024Review
- Coordination of actin plus-end dynamics by IQGAP1, formin, and capping protein.The Journal of cell biology · 2024Article
- Actomyosin organelle functions of SPIRE actin nucleators precede animal evolution.Communications biology · 2024Article
- Coordination of actin plus-end dynamics by IQGAP1, formin, and capping protein.bioRxiv : the preprint server for biology · 2024Article
- Alterations to the broad-spectrum formin inhibitor SMIFH2 modulate potency but not specificity.Scientific reports · 2022Article
- Drosophila Dendritic Arborisation Neurons: Fantastic Actin Dynamics and Where to Find Them.Cells · 2021Review
- Identification of maternal-effect genes in zebrafish using maternal crispants.Development (Cambridge, England) · 2021Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The actin nucleators Spire and Cappuccino synergize to promote actin assembly, but the mechanism of their synergy is controversial. Together these proteins promote the formation of actin meshes, which are conserved structures that regulate the establishment of oocyte polarity. Direct interaction between Spire and Cappuccino is required for oogenesis and for in vitro synergistic actin assembly. This synergy is proposed to be driven by elongation and the formation of a ternary complex at filament barbed ends, or by nucleation and interaction at filament pointed ends. To mimic the geometry of Spire and Cappuccino in vivo, we immobilized Spire on beads and added Cappuccino and actin. Barbed ends, protected by Cappuccino, grow away from the beads while pointed ends are retained, as expected for nucleation-driven synergy. We found that Spire is sufficient to bind barbed ends and retain pointed ends of actin filaments near beads and we identified Spire's barbed-end binding domain. Loss of barbed-end binding increases nucleation by Spire and synergy with Cappuccino in bulk pyrene assays and on beads. Importantly, genetic rescue by the loss-of-function mutant indicates that barbed-end binding is not necessary for oogenesis. Thus, increased nucleation is a critical element of synergy both in vitro and in vivo.
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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.