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  1. Article: Peering through the pore: nuclear pore complex structure, assembly, and function.

    Suntharalingam, Mythili / Wente, Susan R

    Developmental cell

    2003  Volume 4, Issue 6, Page(s) 775–789

    Abstract: Nuclear pore complexes (NPCs) are large proteinaceous assemblies that provide the only known portals for exchanging macromolecules between the nucleus and cytoplasm. This includes the movement of small molecules and the selective, facilitated transport ... ...

    Abstract Nuclear pore complexes (NPCs) are large proteinaceous assemblies that provide the only known portals for exchanging macromolecules between the nucleus and cytoplasm. This includes the movement of small molecules and the selective, facilitated transport of large proteins and RNAs. Faithful, continuous NPC assembly is key for maintaining normal physiological function and is closely tied to proper cell division. This review focuses on the most outstanding issues involving NPC structure, assembly, and function.
    MeSH term(s) Animals ; Biological Transport, Active ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; Humans ; Macromolecular Substances ; Models, Biological ; Nuclear Pore/chemistry ; Nuclear Pore/metabolism ; Nuclear Pore/ultrastructure ; Nuclear Pore Complex Proteins/metabolism ; RNA/metabolism
    Chemical Substances Macromolecular Substances ; Nuclear Pore Complex Proteins ; RNA (63231-63-0)
    Language English
    Publishing date 2003-04-01
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S. ; Review
    ZDB-ID 2054967-2
    ISSN 1878-1551 ; 1534-5807
    ISSN (online) 1878-1551
    ISSN 1534-5807
    DOI 10.1016/s1534-5807(03)00162-x
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 5742: Show issues Location:
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    Zs.MG 76: Show issues

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  2. Article: Nuclear export of the yeast mRNA-binding protein Nab2 is linked to a direct interaction with Gfd1 and to Gle1 function.

    Suntharalingam, Mythili / Alcázar-Román, Abel R / Wente, Susan R

    The Journal of biological chemistry

    2004  Volume 279, Issue 34, Page(s) 35384–35391

    Abstract: Nuclear export of mRNA is mediated by interactions between soluble factors and nuclear pore complex (NPC) proteins. In Saccharomyces cerevisiae, Nab2 is an essential RNA-binding protein that shuttles between the nucleus and cytoplasm. The mechanism for ... ...

    Abstract Nuclear export of mRNA is mediated by interactions between soluble factors and nuclear pore complex (NPC) proteins. In Saccharomyces cerevisiae, Nab2 is an essential RNA-binding protein that shuttles between the nucleus and cytoplasm. The mechanism for trafficking of Nab2-bound mRNA through the NPC has not been defined. Gle1 is also required for mRNA export, and Gle1 interactions with NPC proteins, the RNA helicase Dbp5, and Gfd1 have been reported. Here we report that Nab2, Gfd1, and Gle1 associate in a complex. By using immobilized recombinant Gfd1, Nab2 was isolated from total yeast lysate. A similar biochemical assay with immobilized recombinant Nab2 resulted in coisolation of Gfd1 and Gle1. A Nab2-Gfd1 complex was also identified by coimmunoprecipitation from yeast lysates. In vitro binding assays with recombinant proteins revealed a direct association between Nab2 and Gfd1, and two-hybrid assays delineated Gfd1 binding to the N-terminal Nab2 domain. This N-terminal Nab2 domain is distinct from its RNA binding domains suggesting Nab2 could bind Gfd1 and RNA simultaneously. As Nab2 export was blocked in a gle1 mutant at the restrictive temperature, we propose a model wherein Gfd1 serves as a bridging factor between Gle1 and Nab2-bound mRNA during export.
    MeSH term(s) Active Transport, Cell Nucleus ; Carrier Proteins/metabolism ; Cell Nucleus/metabolism ; Fungal Proteins/metabolism ; Nuclear Pore/metabolism ; Nuclear Pore Complex Proteins ; Nucleocytoplasmic Transport Proteins/metabolism ; Protein Binding ; RNA, Messenger/metabolism ; RNA-Binding Proteins/metabolism ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Temperature
    Chemical Substances Carrier Proteins ; Fungal Proteins ; GLE1 protein, S cerevisiae ; Gfd1 protein, S cerevisiae ; NAB2 protein, S cerevisiae ; Nuclear Pore Complex Proteins ; Nucleocytoplasmic Transport Proteins ; RNA, Messenger ; RNA-Binding Proteins ; Recombinant Proteins ; Saccharomyces cerevisiae Proteins
    Language English
    Publishing date 2004-06-18
    Publishing country United States
    Document type Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M402044200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Uc I Zs.108: Show issues Location:
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  3. Article: Cytoplasmic inositol hexakisphosphate production is sufficient for mediating the Gle1-mRNA export pathway.

    Miller, Aimee L / Suntharalingam, Mythili / Johnson, Sylvia L / Audhya, Anjon / Emr, Scott D / Wente, Susan R

    The Journal of biological chemistry

    2004  Volume 279, Issue 49, Page(s) 51022–51032

    Abstract: Production of inositol hexakisphosphate (IP6) by Ipk1, the inositol-1,3,4,5,6-pentakisphosphate 2-kinase, is required for Gle1-mediated mRNA export in Saccharomyces cerevisiae cells. To examine the network of interactions that require IP6 production, an ... ...

    Abstract Production of inositol hexakisphosphate (IP6) by Ipk1, the inositol-1,3,4,5,6-pentakisphosphate 2-kinase, is required for Gle1-mediated mRNA export in Saccharomyces cerevisiae cells. To examine the network of interactions that require IP6 production, an analysis of fitness defects was conducted in mutants harboring both an ipk1 null allele and a mutant allele in genes encoding nucleoporins or transport factors. Enhanced lethality was observed with a specific subset of mutants, including nup42, nup116, nup159, dbp5, and gle2, all of which had been previously connected to Gle1 function. Complementation of the nup116Deltaipk1Delta and nup42Deltaipk1Delta double mutants did not require the Phe-Gly repeat domains in the respective nucleoporins, suggesting that IP6 was acting subsequent to heterogeneous nuclear ribonucleoprotein targeting to the nuclear pore complex. With Nup42 and Nup159 localized exclusively to the nuclear pore complex cytoplasmic side, we speculated that IP6 may regulate a cytoplasmic step in mRNA export. To test this prediction, the spatial requirements for the production of IP6 were investigated. Restriction of Ipk1 to the cytoplasm did not block IP6 production. Moreover, coincident sequestering of both Ipk1 and Mss4 (an enzyme required for phosphatidylinositol 4,5-bisphosphate production) to the cytoplasm also did not block IP6 production. Given that the kinase required for inositol 1,3,4,5,6-pentakisphosphate production (Ipk2) is localized in the nucleus, these results indicated that soluble inositides were diffusing between the nucleus and the cytoplasm. Additionally, the cytoplasmic production of IP6 by plasma membrane-anchored Ipk1 rescued a gle1-2 ipk1-4 synthetic lethal mutant. Thus, cytoplasmic IP6 production is sufficient for mediating the Gle1-mRNA export pathway.
    MeSH term(s) Active Transport, Cell Nucleus ; Alleles ; Carrier Proteins/physiology ; Cell Membrane/metabolism ; Cell Nucleus/metabolism ; Chromatography, High Pressure Liquid ; Cryoelectron Microscopy ; Cytoplasm/metabolism ; Gene Deletion ; Genetic Complementation Test ; Genetic Vectors ; Genotype ; Green Fluorescent Proteins/chemistry ; Green Fluorescent Proteins/metabolism ; Models, Biological ; Mutation ; Nuclear Pore Complex Proteins/chemistry ; Phenotype ; Phosphotransferases/metabolism ; Phosphotransferases (Alcohol Group Acceptor)/metabolism ; Phytic Acid/metabolism ; Plasmids/metabolism ; Protein Binding ; Protein Structure, Tertiary ; RNA, Messenger/metabolism ; Saccharomyces cerevisiae/metabolism ; Saccharomyces cerevisiae Proteins/metabolism ; Saccharomyces cerevisiae Proteins/physiology ; Temperature ; Time Factors
    Chemical Substances Carrier Proteins ; GLE1 protein, S cerevisiae ; Nuclear Pore Complex Proteins ; RNA, Messenger ; Saccharomyces cerevisiae Proteins ; Green Fluorescent Proteins (147336-22-9) ; Phytic Acid (7IGF0S7R8I) ; Phosphotransferases (EC 2.7.-) ; ARG82 protein, S cerevisiae (EC 2.7.1.-) ; IPK1 protein, S cerevisiae (EC 2.7.1.-) ; Phosphotransferases (Alcohol Group Acceptor) (EC 2.7.1.-) ; MSS4 protein, S cerevisiae (EC 2.7.1.68)
    Language English
    Publishing date 2004-09-30
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M409394200
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Uc I Zs.108: Show issues Location:
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