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    Domain analysis of supervillin, an F-actin bundling plasma membrane protein with functional nuclear localization signals

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    Authors
    Wulfkuhle, J. D.
    Donina, I. E.
    Stark, N. H.
    Pope, Robert K.
    Pestonjamasp, Kersi N.
    Niswonger, M. L.
    Luna, Elizabeth J.
    UMass Chan Affiliations
    Department of Cell Biology
    Document Type
    Journal Article
    Publication Date
    1999-06-11
    Keywords
    Actins
    Animals
    Base Sequence
    Binding Sites
    COS Cells
    Cattle
    Cell Adhesion
    Cell Line
    Cytoskeleton
    DNA Primers
    Gene Expression
    Green Fluorescent Proteins
    Lamins
    Luminescent Proteins
    Membrane Proteins
    Microfilament Proteins
    Nuclear Localization Signals
    Nuclear Proteins
    Phenotype
    Recombinant Fusion Proteins
    Vinculin
    Cell Biology
    Life Sciences
    Medicine and Health Sciences
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    Abstract
    A growing number of actin-associated membrane proteins have been implicated in motile processes, adhesive interactions, and signal transduction to the cell nucleus. We report here that supervillin, an F-actin binding protein originally isolated from bovine neutrophil plasma membranes, contains functional nuclear targeting signals and localizes at or near vinculin-containing focal adhesion plaques in COS7-2 and CV1 cells. Overexpression of full-length supervillin in these cells disrupts the integrity of focal adhesion plaques and results in increased levels of F-actin and vinculin. Localization studies of chimeric proteins containing supervillin sequences fused with the enhanced green fluorescent protein indicate that: (1) the amino terminus promotes F-actin binding, targeting to focal adhesions, and limited nuclear localization; (2) the dominant nuclear targeting signal is in the center of the protein; and (3) the carboxy-terminal villin/gelsolin homology domain of supervillin does not, by itself, bind tightly to the actin cytoskeleton in vivo. Overexpression of chimeras containing both the amino-terminal F-actin binding site(s) and the dominant nuclear targeting signal results in the formation of large nuclear bundles containing F-actin, supervillin, and lamin. These results suggest that supervillin may contribute to cytoarchitecture in the nucleus, as well as at the plasma membrane.
    Source
    J Cell Sci. 1999 Jul;112 ( Pt 13):2125-36. Link to article on publisher's website
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/50775
    PubMed ID
    10362542
    Related Resources
    Link to article in PubMed
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    UMass Chan Faculty and Researcher Publications
    Radiology Publications
    Luna Lab

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