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  1. Article ; Online: Eisosomes and plasma membrane organization.

    Olivera-Couto, Agustina / Aguilar, Pablo S

    Molecular genetics and genomics : MGG

    2012  Volume 287, Issue 8, Page(s) 607–620

    Abstract: Membrane compartmentalization allows the spatial segregation of different functions, such as signal transduction and protein trafficking, and ensures their fidelity and efficiency. Eisosomes constitute nanoscale furrow-like invaginations of the plasma ... ...

    Abstract Membrane compartmentalization allows the spatial segregation of different functions, such as signal transduction and protein trafficking, and ensures their fidelity and efficiency. Eisosomes constitute nanoscale furrow-like invaginations of the plasma membrane where proteins and lipids segregate. The intense interest elicited by eisosomes over the last few years has led to the identification and molecular characterization of their key constituents. This review addresses eisosome structure, functions and its implications for the mechanistic understanding of curvature-induced membrane nanodomains formation and signaling compartmentalization in living cells.
    MeSH term(s) Cell Membrane/chemistry ; Cell Membrane/metabolism ; Endocytosis/physiology ; Fungi/physiology ; Membrane Microdomains/metabolism ; Organelles/chemistry ; Organelles/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Signal Transduction
    Chemical Substances Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2012-07-15
    Publishing country Germany
    Document type Journal Article ; Review
    ZDB-ID 2044817-X
    ISSN 1617-4623 ; 1617-4615
    ISSN (online) 1617-4623
    ISSN 1617-4615
    DOI 10.1007/s00438-012-0706-8
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 1198: Show issues Location:
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  2. Article: Eisosomes and plasma membrane organization

    Olivera-Couto, Agustina / Aguilar, Pablo S

    Molecular genetics and genomics. 2012 Aug., v. 287, no. 8

    2012  

    Abstract: Membrane compartmentalization allows the spatial segregation of different functions, such as signal transduction and protein trafficking, and ensures their fidelity and efficiency. Eisosomes constitute nanoscale furrow-like invaginations of the plasma ... ...

    Abstract Membrane compartmentalization allows the spatial segregation of different functions, such as signal transduction and protein trafficking, and ensures their fidelity and efficiency. Eisosomes constitute nanoscale furrow-like invaginations of the plasma membrane where proteins and lipids segregate. The intense interest elicited by eisosomes over the last few years has led to the identification and molecular characterization of their key constituents. This review addresses eisosome structure, functions and its implications for the mechanistic understanding of curvature-induced membrane nanodomains formation and signaling compartmentalization in living cells.
    Keywords lipids ; plasma membrane ; protein transport ; proteins ; signal transduction
    Language English
    Dates of publication 2012-08
    Size p. 607-620.
    Publishing place Springer-Verlag
    Document type Article
    ISSN 1617-4615
    DOI 10.1007/s00438-012-0706-8
    Database NAL-Catalogue (AGRICOLA)

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  3. Article ; Online: Eisosomes are dynamic plasma membrane domains showing pil1-lsp1 heteroligomer binding equilibrium.

    Olivera-Couto, Agustina / Salzman, Valentina / Mailhos, Milagros / Digman, Michelle A / Gratton, Enrico / Aguilar, Pablo S

    Biophysical journal

    2015  Volume 108, Issue 7, Page(s) 1633–1644

    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. ... ...

    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.
    MeSH term(s) Cell Membrane/metabolism ; Phosphoproteins/metabolism ; Protein Binding ; Protein Subunits/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances LSP1 protein, S cerevisiae ; PIL1 protein, S cerevisiae ; Phosphoproteins ; Protein Subunits ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2015-04-07
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 218078-9
    ISSN 1542-0086 ; 0006-3495
    ISSN (online) 1542-0086
    ISSN 0006-3495
    DOI 10.1016/j.bpj.2015.02.011
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 235: Show issues Location:
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    Zs.MO 2: Show issues

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  4. Article ; Online: The eisosome core is composed of BAR domain proteins.

    Olivera-Couto, Agustina / Graña, Martin / Harispe, Laura / Aguilar, Pablo S

    Molecular biology of the cell

    2011  Volume 22, Issue 13, Page(s) 2360–2372

    Abstract: Eisosomes define sites of plasma membrane organization. In Saccharomyces cerevisiae, eisosomes delimit furrow-like plasma membrane invaginations that concentrate sterols, transporters, and signaling molecules. Eisosomes are static macromolecular ... ...

    Abstract Eisosomes define sites of plasma membrane organization. In Saccharomyces cerevisiae, eisosomes delimit furrow-like plasma membrane invaginations that concentrate sterols, transporters, and signaling molecules. Eisosomes are static macromolecular assemblies composed of cytoplasmic proteins, most of which have no known function. In this study, we used a bioinformatics approach to analyze a set of 20 eisosome proteins. We found that the core components of eisosomes, paralogue proteins Pil1 and Lsp1, are distant homologues of membrane-sculpting Bin/amphiphysin/Rvs (BAR) proteins. Consistent with this finding, purified recombinant Pil1 and Lsp1 tubulated liposomes and formed tubules when the proteins were overexpressed in mammalian cells. Structural homology modeling and site-directed mutagenesis indicate that Pil1 positively charged surface patches are needed for membrane binding and liposome tubulation. Pil1 BAR domain mutants were defective in both eisosome assembly and plasma membrane domain organization. In addition, we found that eisosome-associated proteins Slm1 and Slm2 have F-BAR domains and that these domains are needed for targeting to furrow-like plasma membrane invaginations. Our results support a model in which BAR domain protein-mediated membrane bending leads to clustering of lipids and proteins within the plasma membrane.
    MeSH term(s) Animals ; COS Cells ; Carrier Proteins/chemistry ; Carrier Proteins/metabolism ; Cell Membrane/genetics ; Cell Membrane/metabolism ; Chlorocebus aethiops ; Computational Biology/methods ; Cytoplasm/metabolism ; Cytoskeletal Proteins ; Liposomes/metabolism ; Membrane Lipids/metabolism ; Membrane Proteins/chemistry ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Models, Molecular ; Phosphoproteins/chemistry ; Phosphoproteins/genetics ; Phosphoproteins/metabolism ; Protein Structure, Tertiary ; RNA-Binding Proteins/chemistry ; RNA-Binding Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/chemistry ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism
    Chemical Substances Carrier Proteins ; Cytoskeletal Proteins ; LSP1 protein, S cerevisiae ; Liposomes ; Membrane Lipids ; Membrane Proteins ; PIL1 protein, S cerevisiae ; Phosphoproteins ; RNA-Binding Proteins ; Saccharomyces cerevisiae Proteins ; Slm1 protein, S cerevisiae ; Slm2 protein, S cerevisiae
    Language English
    Publishing date 2011-05-18
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1098979-1
    ISSN 1939-4586 ; 1059-1524
    ISSN (online) 1939-4586
    ISSN 1059-1524
    DOI 10.1091/mbc.E10-12-1021
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2853: Show issues Location:
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    Zs.MO 410: Show issues

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  5. Article ; Online: A plasma-membrane E-MAP reveals links of the eisosome with sphingolipid metabolism and endosomal trafficking.

    Aguilar, Pablo S / Fröhlich, Florian / Rehman, Michael / Shales, Mike / Ulitsky, Igor / Olivera-Couto, Agustina / Braberg, Hannes / Shamir, Ron / Walter, Peter / Mann, Matthias / Ejsing, Christer S / Krogan, Nevan J / Walther, Tobias C

    Nature structural & molecular biology

    2010  Volume 17, Issue 7, Page(s) 901–908

    Abstract: The plasma membrane delimits the cell and controls material and information exchange between itself and the environment. How different plasma-membrane processes are coordinated and how the relative abundance of plasma-membrane lipids and proteins is ... ...

    Abstract The plasma membrane delimits the cell and controls material and information exchange between itself and the environment. How different plasma-membrane processes are coordinated and how the relative abundance of plasma-membrane lipids and proteins is homeostatically maintained are not yet understood. Here, we used a quantitative genetic interaction map, or E-MAP, to functionally interrogate a set of approximately 400 genes involved in various aspects of plasma-membrane biology, including endocytosis, signaling, lipid metabolism and eisosome function. From this E-MAP, we derived a set of 57,799 individual interactions between genes functioning in these various processes. Using triplet genetic motif analysis, we identified a new component of the eisosome, Eis1, and linked the poorly characterized gene EMP70 to endocytic and eisosome function. Finally, we implicated Rom2, a GDP/GTP exchange factor for Rho1 and Rho2, in the regulation of sphingolipid metabolism.
    MeSH term(s) Cell Membrane/genetics ; Cell Membrane/metabolism ; Endocytosis ; Endosomes/genetics ; Endosomes/metabolism ; Genes, Fungal ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/genetics ; Saccharomyces cerevisiae Proteins/metabolism ; Sphingolipids/genetics ; Sphingolipids/metabolism
    Chemical Substances EMP70 protein, S cerevisiae ; Membrane Proteins ; Saccharomyces cerevisiae Proteins ; Sphingolipids
    Language English
    Publishing date 2010-06-06
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 2126708-X
    ISSN 1545-9985 ; 1545-9993
    ISSN (online) 1545-9985
    ISSN 1545-9993
    DOI 10.1038/nsmb.1829
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4101: Show issues Location:
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    Zs.MG 56: Show issues

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  6. Article: Eisosomes and plasma membrane organization

    Olivera-Couto, Agustina / Aguilar, Pablo S.

    Molecular genetics and genomics

    Volume v. 287,, Issue no. 8

    Abstract: Membrane compartmentalization allows the spatial segregation of different functions, such as signal transduction and protein trafficking, and ensures their fidelity and efficiency. Eisosomes constitute nanoscale furrow-like invaginations of the plasma ... ...

    Abstract Membrane compartmentalization allows the spatial segregation of different functions, such as signal transduction and protein trafficking, and ensures their fidelity and efficiency. Eisosomes constitute nanoscale furrow-like invaginations of the plasma membrane where proteins and lipids segregate. The intense interest elicited by eisosomes over the last few years has led to the identification and molecular characterization of their key constituents. This review addresses eisosome structure, functions and its implications for the mechanistic understanding of curvature-induced membrane nanodomains formation and signaling compartmentalization in living cells.
    Keywords protein transport ; lipids ; plasma membrane ; signal transduction ; proteins
    Language English
    Document type Article
    ISSN 1617-4615
    Database AGRIS - International Information System for the Agricultural Sciences and Technology

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