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Eisosome proteins assemble into a membrane scaffold
Spatial organization of membranes into domains of distinct protein and lipid composition is a fundamental feature of biological systems. The plasma membrane is organized in such domains to efficiently orchestrate the many reactions occurring there simultaneously. Despite the almost universal presenc...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
The Rockefeller University Press
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3257569/ https://www.ncbi.nlm.nih.gov/pubmed/22123866 http://dx.doi.org/10.1083/jcb.201104040 |
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author | Karotki, Lena Huiskonen, Juha T. Stefan, Christopher J. Ziółkowska, Natasza E. Roth, Robyn Surma, Michal A. Krogan, Nevan J. Emr, Scott D. Heuser, John Grünewald, Kay Walther, Tobias C. |
author_facet | Karotki, Lena Huiskonen, Juha T. Stefan, Christopher J. Ziółkowska, Natasza E. Roth, Robyn Surma, Michal A. Krogan, Nevan J. Emr, Scott D. Heuser, John Grünewald, Kay Walther, Tobias C. |
author_sort | Karotki, Lena |
collection | PubMed |
description | Spatial organization of membranes into domains of distinct protein and lipid composition is a fundamental feature of biological systems. The plasma membrane is organized in such domains to efficiently orchestrate the many reactions occurring there simultaneously. Despite the almost universal presence of membrane domains, mechanisms of their formation are often unclear. Yeast cells feature prominent plasma membrane domain organization, which is at least partially mediated by eisosomes. Eisosomes are large protein complexes that are primarily composed of many subunits of two Bin–Amphiphysin–Rvs domain–containing proteins, Pil1 and Lsp1. In this paper, we show that these proteins self-assemble into higher-order structures and bind preferentially to phosphoinositide-containing membranes. Using a combination of electron microscopy approaches, we generate structural models of Pil1 and Lsp1 assemblies, which resemble eisosomes in cells. Our data suggest that the mechanism of membrane organization by eisosomes is mediated by self-assembly of its core components into a membrane-bound protein scaffold with lipid-binding specificity. |
format | Online Article Text |
id | pubmed-3257569 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-32575692012-05-28 Eisosome proteins assemble into a membrane scaffold Karotki, Lena Huiskonen, Juha T. Stefan, Christopher J. Ziółkowska, Natasza E. Roth, Robyn Surma, Michal A. Krogan, Nevan J. Emr, Scott D. Heuser, John Grünewald, Kay Walther, Tobias C. J Cell Biol Research Articles Spatial organization of membranes into domains of distinct protein and lipid composition is a fundamental feature of biological systems. The plasma membrane is organized in such domains to efficiently orchestrate the many reactions occurring there simultaneously. Despite the almost universal presence of membrane domains, mechanisms of their formation are often unclear. Yeast cells feature prominent plasma membrane domain organization, which is at least partially mediated by eisosomes. Eisosomes are large protein complexes that are primarily composed of many subunits of two Bin–Amphiphysin–Rvs domain–containing proteins, Pil1 and Lsp1. In this paper, we show that these proteins self-assemble into higher-order structures and bind preferentially to phosphoinositide-containing membranes. Using a combination of electron microscopy approaches, we generate structural models of Pil1 and Lsp1 assemblies, which resemble eisosomes in cells. Our data suggest that the mechanism of membrane organization by eisosomes is mediated by self-assembly of its core components into a membrane-bound protein scaffold with lipid-binding specificity. The Rockefeller University Press 2011-11-28 /pmc/articles/PMC3257569/ /pubmed/22123866 http://dx.doi.org/10.1083/jcb.201104040 Text en © 2011 Karotki et al. This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/). |
spellingShingle | Research Articles Karotki, Lena Huiskonen, Juha T. Stefan, Christopher J. Ziółkowska, Natasza E. Roth, Robyn Surma, Michal A. Krogan, Nevan J. Emr, Scott D. Heuser, John Grünewald, Kay Walther, Tobias C. Eisosome proteins assemble into a membrane scaffold |
title | Eisosome proteins assemble into a membrane scaffold |
title_full | Eisosome proteins assemble into a membrane scaffold |
title_fullStr | Eisosome proteins assemble into a membrane scaffold |
title_full_unstemmed | Eisosome proteins assemble into a membrane scaffold |
title_short | Eisosome proteins assemble into a membrane scaffold |
title_sort | eisosome proteins assemble into a membrane scaffold |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3257569/ https://www.ncbi.nlm.nih.gov/pubmed/22123866 http://dx.doi.org/10.1083/jcb.201104040 |
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