ArticleNature cell biology2012
Patchwork organization of the yeast plasma membrane into numerous coexisting domains.
Article in Nature cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 122 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
122 citing papers in PubMed, 239 citations in OpenAlex.
- Spatial Deconstruction of the Plasma Membrane.Journal of the American Chemical Society · 2026Article
- Phase separation across membranes and condensates in cell organization and function.Nature reviews. Molecular cell biology · 2026Review
- Yeast Membrane Hydration is Maintained Under Ethanol Exposure.The Journal of membrane biology · 2025Article
- Advanced adhesion and targeting strategies to prolong gut residence time and improve eLBP efficacy in colonic diseases.Advanced drug delivery reviews · 2025Review
- Molecular landscape of the fungal plasma membrane and implications for antifungal action.Nature communications · 2025Article
- A Yeast-Based Assay for Inhibitors of l-Lactate Transport Utilizing Fluorescent Biosensors.ChemMedChem · 2025Article
- Functional analysis of Candida albicans Cdr1 through homologous and heterologous expression studies.FEMS yeast research · 2025Review
- Definition of phosphatidylinositol 4,5-bisphosphate distribution by freeze-fracture replica labeling.The Journal of cell biology · 2025Article
- Molecular tipping points in plant cell surface HQuantitative plant biology · 2025Review
- The Cwr1 protein kinase localizes to the plasma membrane and mediates resistance to cell wall stress inmSphere · 2024Article
- Article
- The joint action of yeast eisosomes and membraneless organelles in response to ethanol stress.Heliyon · 2024Article
- Phosphoregulation of the yeast Pma1 H+-ATPase autoinhibitory domain involves the Ptk1/2 kinases and the Glc7 PP1 phosphatase and is under TORC1 control.PLoS genetics · 2024Article
- Inducible degradation-coupled phosphoproteomics identifies PP2AFrontiers in cell and developmental biology · 2024Article
- Article
- Assembly of Cell-Free Synthesized Ion Channel Molecules in Artificial Lipid Bilayer Observed by Atomic Force Microscopy.Membranes · 2023Article
- The phosphatase Glc7 controls the eisosomal response to starvation via post-translational modification of Pil1.Journal of cell science · 2023Article
- Uncovering diffusive states of the yeast membrane protein, Pma1, and how labeling method can change diffusive behavior.The European physical journal. E, Soft matter · 2023Article
- Structural determinants of REMORIN nanodomain formation in anionic membranes.Biophysical journal · 2023Article
- Bioactive and unusual steroids from Penicillium fungi.Phytochemistry · 2023Article
62 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The plasma membrane is made up of lipids and proteins, and serves as an active interface between the cell and its environment. Many plasma-membrane proteins are laterally segregated in the plane of the membrane, but the underlying mechanisms remain controversial. Here we investigate the distribution and dynamics of a representative set of plasma-membrane-associated proteins in yeast cells. These proteins were distributed non-homogeneously in patterns ranging from distinct patches to nearly continuous networks, and these patterns were in turn strongly influenced by the lipid composition of the plasma membrane. Most proteins segregated into distinct domains. However, proteins with similar or identical transmembrane sequences (TMSs) showed a marked tendency to co-localize. Indeed we could predictably relocate proteins by swapping their TMSs. Finally, we found that the domain association of plasma-membrane proteins has an impact on their function. Our results are consistent with self-organization of biological membranes into a patchwork of coexisting domains.
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What OpenQuestion 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 OpenQuestion graph.