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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Yamada, K. M. Yaen, C. Okazaki, K. Sakata, S. Amachi, T. Kioka, N. Kawauchi, T. Aota, S. Akiyama, S. K. |
| Description | Author Affiliation: Kioka N ( Craniofacial Developmental Biology and Regeneration Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, Maryland 20892, USA.) |
| Abstract | Using the yeast two-hybrid system and an in vitro binding assay, we have identified a novel protein termed vinexin as a vinculin-binding protein. By Northern blotting, we identified two types of vinexin mRNA that were 3 and 2 kb in length. Screening for full-length cDNA clones and sequencing indicated that the two mRNA encode 82- and 37-kD polypeptides termed vinexin α and β, respectively. Both forms of vinexin share a common carboxyl-terminal sequence containing three SH3 domains. The larger vinexin α contains an additional amino-terminal sequence. The interaction between vinexin and vinculin was mediated by two SH3 domains of vinexin and the proline-rich region of vinculin. When expressed, vinexin α and β localized to focal adhesions in NIH 3T3 fibroblasts, and to cell–cell junctions in epithelial LLC-PK1 cells. Furthermore, expression of vinexin increased focal adhesion size. Vinexin α also promoted upregulation of actin stress fiber formation. In addition, cell lines stably expressing vinexin β showed enhanced cell spreading on fibronectin. These data identify vinexin as a novel focal adhesion and cell– cell adhesion protein that binds via SH3 domains to the hinge region of vinculin, which can enhance actin cytoskeletal organization and cell spreading. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 1 |
| Volume Number | 144 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 1999-01-11 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Actins Metabolism Adaptor Proteins, Signal Transducing Cytoskeleton Physiology Muscle Proteins Genetics Vinculin Src Homology Domains 3T3 Cells Amino Acid Sequence Animals Binding Sites Cell Line Cell Movement Chromosome Mapping Cloning, Molecular DNA, Complementary Gene Expression Mice Molecular Sequence Data Rabbits Sequence Homology, Amino Acid Swine Tissue Distribution Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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