| pubmed-article:10931873 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10931873 | lifeskim:mentions | umls-concept:C0044602 | lld:lifeskim |
| pubmed-article:10931873 | lifeskim:mentions | umls-concept:C0887870 | lld:lifeskim |
| pubmed-article:10931873 | lifeskim:mentions | umls-concept:C0031621 | lld:lifeskim |
| pubmed-article:10931873 | lifeskim:mentions | umls-concept:C2936824 | lld:lifeskim |
| pubmed-article:10931873 | lifeskim:mentions | umls-concept:C0917705 | lld:lifeskim |
| pubmed-article:10931873 | lifeskim:mentions | umls-concept:C1167622 | lld:lifeskim |
| pubmed-article:10931873 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10931873 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:10931873 | pubmed:dateCreated | 2000-9-5 | lld:pubmed |
| pubmed-article:10931873 | pubmed:abstractText | Focal adhesions are an elaborate network of interconnecting proteins linking actin stress fibers to the extracellular matrix substrate. Modulation of the focal adhesion plaque provides a mechanism for the regulation of cellular adhesive strength. Using interference reflection microscopy, we found that activation of phosphoinositide 3-kinase (PI 3-kinase) by PDGF induces the dissipation of focal adhesions. Loss of this close apposition between the cell membrane and the extracellular matrix coincided with a redistribution of alpha-actinin and vinculin from the focal adhesion complex to the Triton X-100-soluble fraction. In contrast, talin and paxillin remained localized to focal adhesions, suggesting that activation of PI 3-kinase induced a restructuring of the plaque rather than complete dispersion. Furthermore, phosphatidylinositol (3,4, 5)-trisphosphate (PtdIns (3,4,5)-P(3)), a lipid product of PI 3-kinase, was sufficient to induce restructuring of the focal adhesion plaque. We also found that PtdIns (3,4,5)-P(3) binds to alpha-actinin in PDGF-treated cells. Further evidence demonstrated that activation of PI 3-kinase by PDGF induced a decrease in the association of alpha-actinin with the integrin beta subunit, and that PtdIns (3,4,5)-P(3) could disrupt this interaction in vitro. Modification of focal adhesion structure by PI 3-kinase and its lipid product, PtdIns (3,4,5)-P(3), has important implications for the regulation of cellular adhesive strength and motility. | lld:pubmed |
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| pubmed-article:10931873 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10931873 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10931873 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10931873 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10931873 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:10931873 | pubmed:issn | 0021-9525 | lld:pubmed |
| pubmed-article:10931873 | pubmed:author | pubmed-author:GreenwoodJ... | lld:pubmed |
| pubmed-article:10931873 | pubmed:author | pubmed-author:PrestwichG... | lld:pubmed |
| pubmed-article:10931873 | pubmed:author | pubmed-author:TheibertA BAB | lld:pubmed |
