ArticleBiology open2019
YFR016c/Aip5 is part of an actin nucleation complex in yeast.
Article in Biology open, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- A short linear motif, conserved from yeast to human, binds to members of the Spa2 family of cortical scaffold proteins.Journal of cell science · 2026Article
- Aip5 forms a "composite" actin nucleator with Bud6 and caps pointed ends of actin filaments.The Journal of cell biology · 2025Article
- Oligomerization and exocyst coupling underlie Spa2-mediated focusing of polarized growth in fission yeast.Journal of cell science · 2025Article
- Improved tools for live imaging of F-actin structures in yeast.Molecular biology of the cell · 2024Article
- A teamwork promotion of formin-mediated actin nucleation by Bud6 and Aip5 inMolecular biology of the cell · 2022Article
- Type V myosin focuses the polarisome and shapes the tip of yeast cells.The Journal of cell 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
- Orchestrated actin nucleation by theThe Journal of biological chemistry · 2020Article
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The polarisome comprises a network of proteins that organizes polar growth in yeast and filamentous fungi. The yeast formin Bni1 and the actin nucleation-promoting factor Bud6 are subunits of the polarisome that together catalyze the formation of actin cables below the tip of yeast cells. We identified YFR016c (Aip5) as an interaction partner of Bud6 and the polarisome scaffold Spa2. Yeast cells lacking Aip5 display a reduced number of actin cables. Aip5 binds with its N-terminal region to Spa2 and with its C-terminal region to Bud6. Both interactions collaborate to localize Aip5 at bud tip and neck, and are required to stimulate the formation of actin cables. Our experiments characterize Aip5 as a novel subunit of a complex that regulates the number of actin filaments at sites of polar growth.
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