Adhesion Complexes Formed by OVCAR-4 Cells on Laminin 1 Differ from Those Observed on Fibronectin

References

• Abercrombie M., Dunn G. A. Adhesions of fibroblasts to substratum during contact inhibition observed by interference reflection microscopy. Exp. Cell Res. 1975; 92: 57–62
   PubMed Web of Science ®Google Scholar
• Aumailley M., Timpl R., Sonnenberg A. Antibody to integrin a6 subunit specifically inhibits cell-binding to lami-nin fragment 8. Exp. Cell Res. 1990; 188: 55–60
   PubMed Web of Science ®Google Scholar
• Aumailley M., Mann K., von der Mark H., Tlmpl R. Cell attachment properties of collagen VI and Arg-Gly-Asp dependent binding to its α2(VI) and α3(VI) chains. Exp. Cell Res. 1989; 181: 463–474
   PubMed Web of Science ®Google Scholar
• Aumailley M., Gimond C., Rousselle P. Integrin-mediated cellular interactions with laminins. The Laminins, P. Ekblom, R. Timpl. Harwood Academic Publishers. 1995, in press
   Google Scholar
• Briesewitz R., Kern A., Marcantonio E. E. Ligand-dependent and -independent integrin focal contact localization: the role of the a chain cytoplasmic domain. Mol. Biol. Cell 1993; 4: 593–604
   PubMed Web of Science ®Google Scholar
• Burridge K., Fath K., Kelly T., Nuckolls G., Turner C. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell. Biol. 1988; 4: 487–525
   PubMedGoogle Scholar
• Burridge K., Turner C. E., Romer L. H. Tyrosine phosphorylation of paxillin and pp125FAKaccompanies cell adhesion to extracellular matrix: a role in cytoskelatal assembly. J. Cell Biol. 1992; 119: 893–903
   PubMed Web of Science ®Google Scholar
• Clark E. A., Brugge J. S. Integrins and signal transduction pathways : the road taken. Science 1995; 268: 233–239
   PubMed Web of Science ®Google Scholar
• DePasquale J. A., Izzard C. S. Accumulation of talin in nodes at the edge of the lamellipodium and separate incorporation into adhesion plaques at focal contacts. J. Cell Biol. 1991; 113: 1351–1359
   PubMed Web of Science ®Google Scholar
• Duband J. L., Nuckolls G. H., Ishihara A., Hasegawa T., Yamada K. M., Thiery J. P., Jacobson K. Fibronectin receptor exhibits high lateral motility in embryonic locomoting cells but is immobile in focal contacts and fibrillar streaks in stationary cells. J. Cell Biol. 1988; 107: 1385–1396
   PubMed Web of Science ®Google Scholar
• Fath L. R., Edgell J. C-, Burridge K. The distribution of distinct integrins in focal contacts is determined by the substratum composition. J. Cell Sci. 1989; 92: 67–75
   PubMed Web of Science ®Google Scholar
• Geiger B., Volk T., Volberg T., Bendori R. Molecular interactions in adherens-type contacts. J. Cell Sci. 1987; 8: 251–272
   Google Scholar
• Gimond C., Aumailley M. Cellular interactions with the extracellular matrix are coupled to diverse transmembrane signaling pathways. Exp. Cell Res. 1992; 203: 365–373
   PubMed Web of Science ®Google Scholar
• Gimond C., de Melker A., Aumailley M., Sonnenberg A. The cytoplasmic domain of α6A integrin subunit is an vitro substrate for protein kinase C. Exp. Cell Res. 1995; 216: 232–235
   PubMed Web of Science ®Google Scholar
• Hata A., Akita Y., Suzuki K., Ohno S. Functional divergence of protein kinase C (PKC) family members. J. Biol. Chem. 1993; 268: 9122–9129
   PubMed Web of Science ®Google Scholar
• Hyatt S. L., Liao L., Chapline C., Jaken S. Identification and characterization of α-protein kinase C binding proteins in normal and transformed REF52 cells. Biochemistry 1994; 33: 1223–1228
   PubMed Web of Science ®Google Scholar
• Hynes R. O. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 1992; 69: 11–25
   PubMed Web of Science ®Google Scholar
• Jaken S., Leach K., Klauck T. Association of type 3 protein kinase C with focal contacts in rat embryo fibroblasts. J. Cell Biol. 1989; 109: 697–704
   PubMed Web of Science ®Google Scholar
• Johnson R. P., Craig S. W. An intramolecular association between the head and tail domains of vinculin modulates talin binding. J. Biol. Chem. 1994; 269: 12611–12619
   PubMed Web of Science ®Google Scholar
• Johnson R. P., Craig S. W. F-actin binding site masked by the intramolecular association of vinculin head and tail domains. Nature 1995; 373: 261–264
   PubMed Web of Science ®Google Scholar
• Juliano R. L., Haskill S. Signal transduction from the extracellular matrix. J. Cell Biol. 1993; 120: 577–585
   PubMed Web of Science ®Google Scholar
• Izzard C. S., Lochner L. R. Formation of cell-to-substrate contacts during fibroblast motility: an interference-reflexion study. J. Cell Set. 1980; 42: 81–116
   PubMed Web of Science ®Google Scholar
• Kaufmann S., Piekenbrock T., Goldmann W. H., Barmann M., Isenberg G. Talin binds to actin and promotes filament nudeation. FEBS Lett. 1991; 284: 187–191
   PubMed Web of Science ®Google Scholar
• Kassner P. D., Hemler M. E. Interchangeable a chain cytoplasmic domains play a positive role in control of cell adhesion mediated by VLA-4, a β1 integrin. J. Exp. Med. 1993; 178: 649–660
   PubMed Web of Science ®Google Scholar
• Kawaguchi S., Hemler M. E. Role of the α subunit cytoplasmic domain in regulation of adhesive activity mediated by the integrin VLA-2. J. Biol. Chem. 1993; 268: 16279–16285
   PubMed Web of Science ®Google Scholar
• Kornberg L., Earp H. S., Parsons J. T., Schaller M., Juliano R. L. Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J. Biol. Chem. 1992; 267: 23439–23442
   PubMed Web of Science ®Google Scholar
• Krömer M., Rudiger A. H., Jockusch B., Rudiger M. Intramolecular interactions in vinculin control α-actinin binding to the vinculin head. FEBS Lett. 1994; 355: 259–262
   PubMed Web of Science ®Google Scholar
• LaFlamme S. E., Thomas L. A., Yamada S. S., Yamada K. M. Single subunit chimeric integrins as mimics and inhibitors of endogenous integrin functions in receptor localization, cell spreading and migration, and matrix assembly. J. Cell Biol. 1994; 126: 1287–1298
   PubMed Web of Science ®Google Scholar
• Litchfield D. W., Ball E. H. Phosphorylation of the cytoskeletal protein talin by protein kinase C. Biochem. Biophys. Res. Commun. 1986; 134: 1276–1283
   PubMed Web of Science ®Google Scholar
• Lo S. H., Janmey P. A., Hartwig J. H., Chen L. B. Interactions of tensin with actin and identification of its three actin-binding domains. J. Cell Sci. 1994; 125: 1067–1075
   Web of Science ®Google Scholar
• Luna E. J., Hitt A. L. Cytoskeleton-plasma membrane interactions. Science 1992; 258: 955–964
   PubMed Web of Science ®Google Scholar
• Molony L., Burridge K. Molecular shape and self-association of vinculin and metavinculin. J. Cell. Biochem. 1985; 29: 31–36
   PubMed Web of Science ®Google Scholar
• Paulsson M., Aumailley M., Deutzmann R., Timpl R., Beck K., Engel J. Laminin-nidogen complex. Extraction with chelating agents and structural characterization. Eur. J. Biochem. 1987; 166: 11–19
   PubMedGoogle Scholar
• Regen C. M., Horwitz A. F. Dynamics of β1 integrinmediated adhesive contacts in motile fibroblasts. J. Cell Biol. 1992; 119: 1347–1359
   PubMed Web of Science ®Google Scholar
• Rodriguez-Fernandez J. L., Geiger B., Salomon D., Sabanay I., Zöller M., Ben Ze'ev A. Suppression of rumorigenicity in transformed cells after transfection with vinculin cDNA. J. Cell Biol. 1992; 119: 427–438
   PubMed Web of Science ®Google Scholar
• Rousselle P., Aumailley M. Kalinin is more efficient than laminin in promoting adhesion of primary keratinocytes and some other epithelial cells and has a different requirement for integrin receptors. J. Cell Biol. 1994; 125: 205–214
   PubMed Web of Science ®Google Scholar
• Samuels M., Ezzell R. M., Cardozo T. J., Critchley D R., Coll J. L., Adamson E. D. Expression of chicken vinculin complements the adhesion-defective phenotype of a mutant mouse F9 embryonal carcinoma cells. J. Cell Biol. 1993; 121: 909–921
   PubMed Web of Science ®Google Scholar
• Schmidt C. E., Horwitz A. F., Lauffenburger D. A., Sheetz M. P. Integrin-cytoskeletal interactions in migrating fibroblasts are dynamic, asymmetric, and regulated. J. Cell Biol. 1993; 123: 977–991
   PubMed Web of Science ®Google Scholar
• Sonnenberg A., Linders C. J. T., Modderman P. W., Damsky C. H., Aumailley M., Timpl R. Integrin recognition of different cell-binding fragments of laminin (P1, E3, E8) and evidence that α6β1 but not α6β4 functions as a major receptor for fragment E8. J. Cell Biol. 1990; 110: 2145–2155
   PubMed Web of Science ®Google Scholar
• Sonnenberg A., Gehlsen K. R., Aumailley M., Timpl R. Isolation of α6β1 integrins from platelets and tumor cells by affinity chromatography on mouse laminin fragment E8 and human laminin and localization of this complex in adhesion plaques. Exp. Cell Res. 1991; 197: 234–244
   PubMed Web of Science ®Google Scholar
• Turner C. E., Pavalko F. M., Burridge K. The role of phosphorylation and limited proteolytic cleavage of talin and vinculin in the disruption of focal adhesion integrity. J. Biol. Chem. 1989; 264: 11938–11944
   PubMed Web of Science ®Google Scholar
• Turner C. E., Miller J. T. Primary sequence of paxillin contains putative SH2 and SH3 domain binding motifs and multiple LIM domains: identification of a vinculin and pp125FAK-binding region. J. Cell Sci. 1994; 107: 1583–1591
   PubMed Web of Science ®Google Scholar
• Volberg T., Geiger B., Kam Z., Pankov R., Simcha I., Sabanay H., Coll J. C., Adamson E., Ben Ze'ev A. Focal adhesion formation by F9 embryonal carcinoma cells after vinculin gene disruption. J. Cell Sci. 1995; 108: 2253–2260
   PubMed Web of Science ®Google Scholar
• Vuori K., Ruoslahti E. Activation of protein kinase C precedes α5β1 integrin-mediated cell spreading on fibronectin. J. Biol. Chem. 1993; 268: 21459–21462
   PubMed Web of Science ®Google Scholar
• Weber I., Wallraff E., Albrecht R., Gerisch G. Motility and substratum adhesion of Dictyostelium wild-type and cytoskeletal mutant cells: a study by RICM/bright-field double-view image analysis. J. Cell Sci. 1995; 108: 1519–1530
   PubMed Web of Science ®Google Scholar
• Werth D. K., Pastan I. Vinculin phosphorylation in response to calcium and phorbol esters in intact cells. J. Biol. Chem. 1984; 258: 11423–11426
   Google Scholar
• Wetsel W., Khan W. A., Merchenthaler I., Rivera H., Halpern A., Phung H. M., Negro-Vilar A., Hannun Y. A. Tissue and cellular distribution of the extended family of protein kinase C isoenzymes. J. Cell Biol. 1992; 117: 121–133
   PubMed Web of Science ®Google Scholar
• Wood C. K., Turner C. E., Jackson P., Critchley D. R. Characterization of the paxillin-binding site and the C-terminal focal adhesion targeting sequence in vinculin. J. Cell Sci. 1994; 107: 709–717
   PubMed Web of Science ®Google Scholar
• Woods A., Couchman J. R. Protein kinase C involvement in focal adhesion formation. J. Cell Sci. 1992; 101: 277–290
   PubMed Web of Science ®Google Scholar
• Zachary I., Rozengurt E. Focal adhesion kinase (pp125FAK): a point convergence in the action of neuropeptides, integrins, and oncogenes. Cell 1992; 71: 891–894
   PubMed Web of Science ®Google Scholar