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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Yoshida, M. Mohri, H. Ohno, S. Kanamori, H. Ishigatsubo, Y. Yamaji, S. Koide, Y. Sugiyama, Y. Suzuki, A. |
| Description | Author Affiliation: Yamaji S ( The First Department of Internal Medicine, Yokohama City University School of Medicine, Yokohama 236-0004, Japan.) |
| Abstract | Focal adhesions (FAs) are essential structures for cell adhesion, migration, and morphogenesis. Integrin-linked kinase (ILK), which is capable of interacting with the cytoplasmic domain of β1 integrin, seems to be a key component of FAs, but its exact role in cell–substrate interaction remains to be clarified. Here, we identified a novel ILK-binding protein, affixin, that consists of two tandem calponin homology domains. In CHOcells, affixin and ILK colocalize at FAs and at the tip of the leading edge, whereas in skeletal muscle cells they colocalize at the sarcolemma where cells attach to the basal lamina, showing a striped pattern corresponding to cytoplasmic Z-band striation. When CHO cells are replated on fibronectin, affixin and ILK but not FA kinase and vinculin concentrate at the cell surface in blebs during the early stages of cell spreading, which will grow into membrane ruffles on lamellipodia. Overexpression of the COOH-terminal region of affixin, which is phosphorylated by ILK in vitro, blocks cell spreading at the initial stage, presumably by interfering with the formation of FAs and stress fibers. The coexpression of ILK enhances this effect. These results provide evidence suggesting that affixin is involved in integrin–ILK signaling required for the establishment of cell–substrate adhesion. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 6 |
| Volume Number | 153 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 2001-06-11 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Actinin Calcium-Binding Proteins Metabolism Protein-Serine-Threonine Kinases Proteins Amino Acid Sequence Animals CHO Cells Genetics Cloning, Molecular Cricetinae Focal Adhesions Physiology Gene Expression Microfilament Proteins Molecular Sequence Data Muscle, Skeletal Sarcolemma Sequence Homology, Amino Acid Substrate Specificity Tissue Distribution Research Support, Non-U.S. Gov't Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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