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  • 1
    Keywords: BINDING ; breast cancer ; BREAST-CANCER ; CORE HISTONES ; EXPORT ; NUCLEAR IMPORT ; NUCLEOCYTOPLASMIC TRANSPORT ; PORE COMPLEX ; PROTEIN IMPORT ; RAN ; nuclear pore complex ; DBC-1 ; DMAP-1 ; E3 LIGASE ACTIVITY ; NPC ; Nup358 ; RANGAP1
    Abstract: In vertebrates, the nuclear pore complex (NPC), the gate for transport of macromolecules between the nucleus and the cytoplasm, consists of approximately 30 different nucleoporins (Nups). The Nup and SUMO E3-ligase Nup358/RanBP2 are the major components of the cytoplasmic filaments of the NPC. In this study, we perform a structure-function analysis of Nup358 and describe its role in nuclear import of specific proteins. In a screen for nuclear proteins that accumulate in the cytoplasm upon Nup358 depletion, we identified proteins that were able to interact with Nup358 in a receptor-independent manner. These included the importin alpha/beta-cargo DBC-1 (deleted in breast cancer 1) and DMAP-1 (DNA methyltransferase 1 associated protein 1). Strikingly, a short N-terminal fragment of Nup358 was sufficient to promote import of DBC-1, whereas DMAP-1 required a larger portion of Nup358 for stimulated import. Neither the interaction of RanGAP with Nup358 nor its SUMO-E3 ligase activity was required for nuclear import of all tested cargos. Together, Nup358 functions as a cargo- and receptor-specific assembly platform, increasing the efficiency of nuclear import of proteins through various mechanisms.
    Type of Publication: Journal article published
    PubMed ID: 21995724
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  • 2
    Keywords: RECEPTOR ; CELLS ; EXPRESSION ; CELL ; Germany ; human ; PATHWAY ; SYSTEM ; GENE ; GENES ; PROTEIN ; LINES ; ACTIVATION ; MARKER ; T cell ; T cell activation ; T cells ; T-CELL ; T-CELLS ; BINDING ; CELL-LINES ; SIGNAL ; virus ; IDENTIFICATION ; NUMBER ; CELL-LINE ; LINE ; HUMAN-IMMUNODEFICIENCY-VIRUS ; representational difference analysis ; GENE-PRODUCT ; SUBSET ; PRODUCTS ; HIV ; IMMUNODEFICIENCY VIRUS ; NUCLEOCYTOPLASMIC TRANSPORT ; TAP ; 60S RIBOSOMAL-SUBUNITS ; CD83 ; CRM1 ; IMMUNODEFICIENCY-VIRUS REV ; LEPTOMYCIN B ; RAN ; RECEPTOR CRM1 ; RNA export
    Abstract: In metazoans, the nuclear export of bulk mRNAs is mediated by the export receptor TAP, together with its binding partner p15. A number of viral mRNAs, including the unspliced and partially spliced mRNA species of the human immunodeficiency virus (HIV), however, use an alternative export route via the importin beta-related export receptor CRM1. This raises the question of whether a subset of cellular mRNAs might be exported by CRM1 as well. To identify such mRNAs, we performed a systematic screen in different cell lines, using representational difference analyses of cDNA (cDNA-RDA). In HeLa and Cl-4 cells no cellular transcripts could be identified as exported via CRM1. In contrast, we found a number of CRM1-dependent mRNAs in Jurkat T cells, most of which are induced during a T cell response. One of the identified gene products, the dendritic cell marker CD83, was analyzed in detail. CD83 expression depends on a functional CRM1 pathway in activated Jurkat T cells as well as in a heterologous expression system, independent of activation. Our results point to an important role of the CRM1-dependent export pathway for the expression of CD83 and other genes under conditions of T cell activation. (c) 2006 Elsevier Ltd. All rights reserved
    Type of Publication: Journal article published
    PubMed ID: 16580684
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  • 3
    Publication Date: 2018-07-03
    Description: Importin 13 is a member of the importin β family of transport receptors. Unlike most family members, importin 13 mediates both, nuclear protein import and export. To search for novel importin 13 cargoes, we used stable isotope labeling of amino acids in cell culture (SILAC) and mass spectrometry. Using stringent criteria, we identified 255 importin 13 substrates, including the known cargoes Ubc9, Mago and eIF1A, and validate many of them as transport cargoes by extensive biochemical and cell biological characterization. Several novel cargoes can also be transported by the export receptor CRM1, demonstrating a clear redundancy in receptor choice. Using importin 13 mutants, we show that many of the novel substrates contact regions on the transport receptor that are not used by Ubc9, Mago or eIF1A. Together, this study significantly expands the repertoire of importin 13 cargoes and sets the basis for a more detailed characterization of this extremely versatile transport receptor.
    Print ISSN: 1535-9476
    Electronic ISSN: 1535-9484
    Topics: Biology , Medicine
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