ArticleBiophysical journal2015
Eisosomes are dynamic plasma membrane domains showing pil1-lsp1 heteroligomer binding equilibrium.
Article in Biophysical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 28 citations in OpenAlex.
- Protein dimerization in 2D vs 3D: Geometric allostery enhances binding affinity.The Journal of chemical physics · 2025Article
- Inducible degradation-coupled phosphoproteomics identifies PP2AFrontiers in cell and developmental biology · 2024Article
- The phosphatase Glc7 controls the eisosomal response to starvation via post-translational modification of Pil1.Journal of cell science · 2023Article
- Complementation of an Eisosomal YeastJournal of fungi (Basel, Switzerland) · 2023Article
- Eisosome disruption by noncoding RNA deletion increases protein secretion in yeast.PNAS nexus · 2022Article
- Thermodynamics and Free Energy Landscape of BAR-Domain Dimerization from Molecular Simulations.The journal of physical chemistry. B · 2021Article
- Plasma Membrane MCC/Eisosome Domains Promote Stress Resistance in Fungi.Microbiology and molecular biology reviews : MMBR · 2020Review
- Using enhanced number and brightness to measure protein oligomerization dynamics in live cells.Nature protocols · 2019Article
- Correlative Microscopy of Vitreous Sections Provides Insights into BAR-Domain Organization In Situ.Structure (London, England : 1993) · 2018Article
- MCC/Eisosomes Regulate Cell Wall Synthesis and Stress Responses in Fungi.Journal of fungi (Basel, Switzerland) · 2017Review
- Single-molecule imaging of the BAR-domain protein Pil1p reveals filament-end dynamics.Molecular biology of the cell · 2017Article
- Eisosome Ultrastructure and Evolution in Fungi, Microalgae, and Lichens.Eukaryotic cell · 2015Article
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Authors and funding
6 authors at 4 institutions in 4 countries.
Funding
Abstract
Eisosomes are plasma membrane domains concentrating lipids, transporters, and signaling molecules. In the budding yeast Saccharomyces cerevisiae, these domains are structured by scaffolds composed mainly by two cytoplasmic proteins Pil1 and Lsp1. Eisosomes are immobile domains, have relatively uniform size, and encompass thousands of units of the core proteins Pil1 and Lsp1. In this work we used fluorescence fluctuation analytical methods to determine the dynamics of eisosome core proteins at different subcellular locations. Using a combination of scanning techniques with autocorrelation analysis, we show that Pil1 and Lsp1 cytoplasmic pools freely diffuse whereas an eisosome-associated fraction of these proteins exhibits slow dynamics that fit with a binding-unbinding equilibrium. Number and brightness analysis shows that the eisosome-associated fraction is oligomeric, while cytoplasmic pools have lower aggregation states. Fluorescence lifetime imaging results indicate that Pil1 and Lsp1 directly interact in the cytoplasm and within the eisosomes. These results support a model where Pil1-Lsp1 heterodimers are the minimal eisosomes building blocks. Moreover, individual-eisosome fluorescence fluctuation analysis shows that eisosomes in the same cell are not equal domains: while roughly half of them are mostly static, the other half is actively exchanging core protein subunits.
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