ArticleNature communications2019
Polarisome scaffolder Spa2-mediated macromolecular condensation of Aip5 for actin polymerization.
Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed.
- The complex subunit VdAP-2α regulates polar growth, ergosterol metabolism, and virulence inVirulence · 2026Article
- SH3BGRL proteins are thioredoxin fold-containing actin filament pointed end capping proteins (TPECs).Scientific reports · 2026Article
- Aip5 forms a "composite" actin nucleator with Bud6 and caps pointed ends of actin filaments.The Journal of cell biology · 2025Article
- The origin of septin ring size control in budding yeast.The EMBO journal · 2025Article
- Phase Separation-Regulated Fungal Growth, Sexual Development, Adaptation and Synthetic Biology Applications.Journal of fungi (Basel, Switzerland) · 2025Review
- Oligomerization and exocyst coupling underlie Spa2-mediated focusing of polarized growth in fission yeast.Journal of cell science · 2025Article
- Hyssopus officinalis: MicroRNA-mediated regulation of terpenoid biosynthesis and defense metabolites.Planta · 2025Article
- The phase-separating Magnaporthe oryzae MoSpa2 complex organizes actin nucleation centers for plant infection.The Plant cell · 2025Article
- The roles of yeast formins and their regulators Bud6 and Bil2 in the pheromone response.Molecular biology of the cell · 2024Article
- Spa2 remodels ADP-actin via molecular condensation under glucose starvation.Nature communications · 2024Article
- Rapid evolution of an adaptive multicellular morphology of Candida auris during systemic infection.Nature communications · 2024Article
- Exploring the Role of the Plant Actin Cytoskeleton: From Signaling to Cellular Functions.International journal of molecular sciences · 2023Review
- Advanced imaging techniques for studying protein phase separation in living cells and at single-molecule level.Current opinion in chemical biology · 2023Review
- Interplay of self-organization of microtubule asters and crosslinking protein condensates.PNAS nexus · 2023Article
- Phase separation in fungi.Nature microbiology · 2023Review
- Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022Review
- Condensation of the fusion focus by the intrinsically disordered region of the formin Fus1 is essential for cell-cell fusion.Current biology : CB · 2022Article
- Stage-Specific Genetic Interaction betweenInternational journal of molecular sciences · 2022Article
- A two-component protein condensate of the EGFR cytoplasmic tail and Grb2 regulates Ras activation by SOS at the membrane.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- A teamwork promotion of formin-mediated actin nucleation by Bud6 and Aip5 inMolecular biology of the cell · 2022Article
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Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A multiprotein complex polarisome nucleates actin cables for polarized cell growth in budding yeast and filamentous fungi. However, the dynamic regulations of polarisome proteins in polymerizing actin under physiological and stress conditions remains unknown. We identify a previously functionally unknown polarisome member, actin-interacting-protein 5 (Aip5), which promotes actin assembly synergistically with formin Bni1. Aip5-C terminus is responsible for its activities by interacting with G-actin and Bni1. Through N-terminal intrinsically disordered region, Aip5 forms high-order oligomers and generate cytoplasmic condensates under the stresses conditions. The molecular dynamics and reversibility of Aip5 condensates are regulated by scaffolding protein Spa2 via liquid-liquid phase separation both in vitro and in vivo. In the absence of Spa2, Aip5 condensates hamper cell growth and actin cable structures under stress treatment. The present study reveals the mechanisms of actin assembly for polarity establishment and the adaptation in stress conditions to protect actin assembly by protein phase separation.
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