UMMS Affiliation

Department of Cell Biology

Date

6-11-1999

Document Type

Article

Subjects

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

Disciplines

Cell Biology | Life Sciences | Medicine and Health Sciences

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.

Rights and Permissions

Citation: J Cell Sci. 1999 Jul;112 ( Pt 13):2125-36. Link to article on publisher's website

Related Resources

Link to article in PubMed

PubMed ID

10362542

Share

COinS
 
 

To view the content in your browser, please download Adobe Reader or, alternately,
you may Download the file to your hard drive.

NOTE: The latest versions of Adobe Reader do not support viewing PDF files within Firefox on Mac OS and if you are using a modern (Intel) Mac, there is no official plugin for viewing PDF files within the browser window.