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    Intermolecular masking of the HIV-1 Rev NLS by the cellular protein HIC: novel insights into the regulation of Rev nuclear import.

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    Authors
    Gu, Lili
    Tsuji, Takahiro
    Jarboui, Mohamed Ali
    Yeo, Geok P
    Sheehy, Noreen
    Hall, William W
    Gautier, Virginie W
    Affiliation
    UCD-Centre for Research in Infectious Diseases, School of Medicine and Medical Science, University College Dublin (UCD), Belfield, Dublin 4, Ireland.
    Issue Date
    2011
    MeSH
    Active Transport, Cell Nucleus
    Animals
    COS Cells
    Cell Line
    Cell Nucleus
    Cercopithecus aethiops
    Gene Expression Regulation, Viral
    HIV-1
    Hela Cells
    Humans
    Jurkat Cells
    Karyopherins
    Myogenic Regulatory Factors
    Nuclear Localization Signals
    Protein Binding
    U937 Cells
    beta Karyopherins
    rev Gene Products, Human Immunodeficiency Virus
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    Citation
    Intermolecular masking of the HIV-1 Rev NLS by the cellular protein HIC: novel insights into the regulation of Rev nuclear import. 2011, 8:17 Retrovirology
    Journal
    Retrovirology
    URI
    http://hdl.handle.net/10147/135955
    DOI
    10.1186/1742-4690-8-17
    PubMed ID
    21401918
    Additional Links
    http://www.ncbi.nlm.nih.gov/pubmed/21401918
    Abstract
    The HIV-1 regulatory protein Rev, which is essential for viral replication, mediates the nuclear export of unspliced viral transcripts. Rev nuclear function requires active nucleocytoplasmic shuttling, and Rev nuclear import is mediated by the recognition of its Nuclear Localisation Signal (NLS) by multiple import factors, which include transportin and importin β. However, it remains unclear which nuclear import pathway(s) predominate in vivo, and the cellular environment that modulates Rev nucleocytoplasmic shuttling remains to be characterised.
    In our study, we have identified the cellular protein HIC (Human I-mfa domain-Containing protein) as a novel interactor of HIV-1 Rev. We demonstrate that HIC selectively interferes with Rev NLS interaction with importin β and impedes its nuclear import and function, but does not affect Rev nuclear import mediated by transportin. Hence, the molecular determinants mediating Rev-NLS recognition by importin β and transportin appear to be distinct. Furthermore, we have employed HIC and M9 M, a peptide specifically designed to inhibit the transportin-mediated nuclear import pathway, to characterise Rev nuclear import pathways within different cellular environments. Remarkably, we could show that in 293T, HeLa, COS7, Jurkat, U937, THP-1 and CEM cells, Rev nuclear import is cell type specific and alternatively mediated by transportin or importin β, in a mutually exclusive fashion.
    Rev cytoplasmic sequestration by HIC may represent a novel mechanism for the control of Rev function. These studies highlight that the multivalent nature of the Rev NLS for different import receptors enables Rev to adapt its nuclear trafficking strategy.
    Item Type
    Article
    Language
    en
    ISSN
    1742-4690
    ae974a485f413a2113503eed53cd6c53
    10.1186/1742-4690-8-17
    Scopus Count
    Collections
    Publications

    entitlement

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