ArticleThe Journal of cell biology2021
Type V myosin focuses the polarisome and shapes the tip of yeast cells.
Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 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
- Oligomerization and exocyst coupling underlie Spa2-mediated focusing of polarized growth in fission yeast.Journal of cell science · 2025Article
- Cargo adaptors use a handhold mechanism to engage with myosin V for organelle transport.The Journal of cell biology · 2025Article
- Interface integrity in septin protofilaments is maintained by an arginine residue conserved from yeast to man.Molecular biology of the cell · 2025Article
- Exocytic plasma membrane flows remodel endoplasmic reticulum-plasma membrane tethering for septin collar assembly.Science advances · 2024Article
- Transient septin sumoylation steers a Fir1-Skt5 protein complex between the split septin ring.The Journal of cell biology · 2024Article
- Artificial Hsp104-mediated systems for re-localizing protein aggregates.Nature communications · 2023Article
- Article
- Cargo Recognition Mechanisms of Yeast Myo2 Revealed by AlphaFold2-Powered Protein Complex Prediction.Biomolecules · 2022Article
- A positive feedback loop involving the Spa2 SHD domain contributes to focal polarization.PloS one · 2022Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
The polarisome is a cortical proteinaceous microcompartment that organizes the growth of actin filaments and the fusion of secretory vesicles in yeasts and filamentous fungi. Polarisomes are compact, spotlike structures at the growing tips of their respective cells. The molecular forces that control the form and size of this microcompartment are not known. Here we identify a complex between the polarisome subunit Pea2 and the type V Myosin Myo2 that anchors Myo2 at the cortex of yeast cells. We discovered a point mutation in the cargo-binding domain of Myo2 that impairs the interaction with Pea2 and consequently the formation and focused localization of the polarisome. Cells carrying this mutation grow round instead of elongated buds. Further experiments and biophysical modeling suggest that the interactions between polarisome-bound Myo2 motors and dynamic actin filaments spatially focus the polarisome and sustain its compact shape.
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What Socratic holds
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 Socratic graph.