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• W1997700910 abstract "The integrin alpha3beta1 mediates cellular adhesion to the matrix ligand laminin-5. A second integrin ligand, the urokinase receptor (uPAR), associates with alpha3beta1 via a surface loop within the alpha3 beta-propeller (residues 242-246) but outside the laminin binding region, suggesting that uPAR-integrin interactions could signal differently from matrix engagement. To explore this, alpha3-/- epithelial cells were reconstituted with wild-type (wt) alpha3 or alpha3 with Ala mutations within the uPAR-interacting loop (H245A or R244A). Wt or mutant-bearing cells showed comparable expression and adhesion to laminin-5. Cells expressing wt alpha3 and uPAR dissociated in culture, with increased Src activity, up-regulation of SLUG, and down-regulation of E-cadherin and gamma-catenin. Src kinase inhibition or expression of Src 1-251 restored the epithelial phenotype. The H245A and R244A mutants were unaffected by coexpression of uPAR. We conclude that alpha3beta1 regulates both cell-cell contact and matrix adhesion, but through distinct protein interaction sites within its beta-propeller. These studies reveal an integrin- and Src-dependent pathway for SLUG expression and mesenchymal transition." @default.
• W1997700910 created "2016-06-24" @default.
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• W1997700910 date "2003-10-13" @default.
• W1997700910 modified "2023-09-27" @default.
• W1997700910 title "Distinct ligand binding sites in integrin α3β1 regulate matrix adhesion and cell–cell contact" @default.
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• W1997700910 doi "https://doi.org/10.1083/jcb.200304065" @default.
• W1997700910 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2173444" @default.
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