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    Functional analysis of Tpr: identification of nuclear pore complex association and nuclear localization domains and a role in mRNA export

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    Authors
    Bangs, Peter Lawrence
    Burke, Brian
    Powers, Christine M.
    Craig, Roger W.
    Purohit, Aruna
    Doxsey, Stephen J.
    UMass Chan Affiliations
    Department of Cell Biology
    Program in Molecular Medicine
    Document Type
    Journal Article
    Publication Date
    1998-12-29
    Keywords
    Animals
    Biological Transport
    COS Cells
    Cell Line
    Cell Nucleus
    Cricetinae
    Hela Cells
    Humans
    Immunohistochemistry
    Kidney
    Macromolecular Substances
    Mesocricetus
    Microscopy, Fluorescence
    Microscopy, Immunoelectron
    Models, Biological
    Nuclear Envelope
    Nuclear Pore Complex Proteins
    Nuclear Proteins
    Protein Binding
    *Protein Structure, Tertiary
    Proteins
    Proto-Oncogene Proteins
    RNA, Messenger
    Sequence Deletion
    Structure-Activity Relationship
    Transfection
    Cell Biology
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    Abstract
    Tpr is a 270-kD coiled-coil protein localized to intranuclear filaments of the nuclear pore complex (NPC). The mechanism by which Tpr contributes to the structure and function of the nuclear pore is currently unknown. To gain insight into Tpr function, we expressed the full-length protein and several subdomains in mammalian cell lines and examined their effects on nuclear pore function. Through this analysis, we identified an NH2-terminal domain that was sufficient for association with the nucleoplasmic aspect of the NPC. In addition, we unexpectedly found that the acidic COOH terminus was efficiently transported into the nuclear interior, an event that was apparently mediated by a putative nuclear localization sequence. Ectopic expression of the full-length Tpr caused a dramatic accumulation of poly(A)+ RNA within the nucleus. Similar results were observed with domains that localized to the NPC and the nuclear interior. In contrast, expression of these proteins did not appear to affect nuclear import. These data are consistent with a model in which Tpr is tethered to intranuclear filaments of the NPC by its coiled coil domain leaving the acidic COOH terminus free to interact with soluble transport factors and mediate export of macromolecules from the nucleus.
    Source
    J Cell Biol. 1998 Dec 28;143(7):1801-12.
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/42604
    PubMed ID
    9864356
    Related Resources
    Link to Article in PubMed
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    UMass Chan Faculty and Researcher Publications
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