Eisosome proteins assemble into a membrane scaffold
| العنوان: | Eisosome proteins assemble into a membrane scaffold |
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| المؤلفون: | John E. Heuser, Robyn Roth, Tobias C. Walther, Scott D. Emr, Lena Karotki, Michal A. Surma, Juha T. Huiskonen, Natasza E. Ziółkowska, Kay Grünewald, Nevan J. Krogan, Christopher J. Stefan |
| المصدر: | The Journal of Cell Biology |
| سنة النشر: | 2011 |
| مصطلحات موضوعية: | Scaffold protein, Vesicle-associated membrane protein 8, Saccharomyces cerevisiae Proteins, Saccharomyces cerevisiae, Article, 03 medical and health sciences, 0302 clinical medicine, Protein structure, Integral membrane protein, Research Articles, Eisosome, 030304 developmental biology, 0303 health sciences, biology, Membrane transport protein, Cell Membrane, Peripheral membrane protein, Cell Biology, Phosphoproteins, Recombinant Proteins, Protein Structure, Tertiary, 3. Good health, Cell biology, Membrane protein, biology.protein, 030217 neurology & neurosurgery |
| الوصف: | Membrane organization by eisosomes is mediated by self-assembly of its main components into a membrane-bound protein scaffold with lipid-binding specificity. 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. |
| اللغة: | English |
| تدمد: | 1540-8140 0021-9525 |
| URL الوصول: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::65017cd682fe5f0155d813e4f07b125b http://ora.ox.ac.uk/objects/uuid:3f87bf9f-b232-4d66-b256-4b0774ce50f1 |
| حقوق: | OPEN |
| رقم الأكسشن: | edsair.doi.dedup.....65017cd682fe5f0155d813e4f07b125b |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 15408140 00219525 |
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