Vinculin acts as a sensor in lipid regulation of adhesion-site turnover
The dynamics of cell adhesion sites control cell morphology and motility. Adhesion-site turnover is thought to depend on the local availability of the acidic phospholipid phosphatidylinositol-4,5-bisphosphate (PIP₂). PIP₂ can bind to many cell adhesion proteins such as vinculin and talin, but the co...
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| Veröffentlicht in: | Journal of cell science 2005-04, Vol.118 (7), p.1461-1472 |
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| container_title | Journal of cell science |
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| creator | Chandrasekar, Indra Stradal, Theresia E. B Holt, Mark R Entschladen, Frank Jockusch, Brigitte M Ziegler, Wolfgang H |
| description | The dynamics of cell adhesion sites control cell morphology and motility. Adhesion-site turnover is thought to depend on the local availability of the acidic phospholipid phosphatidylinositol-4,5-bisphosphate (PIP₂). PIP₂ can bind to many cell adhesion proteins such as vinculin and talin, but the consequences of this interaction are poorly understood. To study the significance of phospholipid binding to vinculin for adhesion-site turnover and cell motility, we constructed a mutant, vinculin-LD, deficient in acidic phospholipid binding yet with functional actin-binding sites. When expressed in cells, vinculin-LD was readily recruited to adhesion sites, as judged by fluorescence recovery after photobleaching (FRAP) analysis, but cell spreading and migration were strongly impaired, and PIP₂-dependent disassembly of adhesions was suppressed. Thus, PIP₂ binding is not essential for vinculin activation and recruitment, as previously suggested. Instead, we propose that PIP₂ levels can regulate the uncoupling of adhesion sites from the actin cytoskeleton, with vinculin functioning as a sensor. |
| doi_str_mv | 10.1242/jcs.01734 |
| format | Article |
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When expressed in cells, vinculin-LD was readily recruited to adhesion sites, as judged by fluorescence recovery after photobleaching (FRAP) analysis, but cell spreading and migration were strongly impaired, and PIP₂-dependent disassembly of adhesions was suppressed. Thus, PIP₂ binding is not essential for vinculin activation and recruitment, as previously suggested. 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When expressed in cells, vinculin-LD was readily recruited to adhesion sites, as judged by fluorescence recovery after photobleaching (FRAP) analysis, but cell spreading and migration were strongly impaired, and PIP₂-dependent disassembly of adhesions was suppressed. Thus, PIP₂ binding is not essential for vinculin activation and recruitment, as previously suggested. 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To study the significance of phospholipid binding to vinculin for adhesion-site turnover and cell motility, we constructed a mutant, vinculin-LD, deficient in acidic phospholipid binding yet with functional actin-binding sites. When expressed in cells, vinculin-LD was readily recruited to adhesion sites, as judged by fluorescence recovery after photobleaching (FRAP) analysis, but cell spreading and migration were strongly impaired, and PIP₂-dependent disassembly of adhesions was suppressed. Thus, PIP₂ binding is not essential for vinculin activation and recruitment, as previously suggested. Instead, we propose that PIP₂ levels can regulate the uncoupling of adhesion sites from the actin cytoskeleton, with vinculin functioning as a sensor.</abstract><cop>England</cop><pmid>15769850</pmid><doi>10.1242/jcs.01734</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Company of Biologists |
| subjects | Animals Binding Sites - physiology Cell Adhesion - physiology Cell Line, Tumor Cell Movement - physiology Cloning, Molecular Collagen - metabolism Extracellular Matrix - metabolism Fluorescence Recovery After Photobleaching Green Fluorescent Proteins - metabolism Ligands Mice Mutagenesis, Site-Directed Mutation Phosphatidylinositol 4,5-Diphosphate - metabolism Phosphotransferases (Alcohol Group Acceptor) - genetics Phosphotransferases (Alcohol Group Acceptor) - metabolism Protein Conformation Vinculin - chemistry Vinculin - genetics Vinculin - metabolism |
| title | Vinculin acts as a sensor in lipid regulation of adhesion-site turnover |
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