Targeting of Cytoskeletal Linker Proteins to Focal Adhesion Complexes is Reduced in Fibroblasts Adhering to Laminin-1 when Compared to Fibronectin

References

• Abercrombie M., Heaysman J., Pegrum S. M. The locomotion of fibroblasts in culture. Exp. Cell Res. 1971; 65: 359–367
   PubMed Web of Science ®Google Scholar
• Aumailley M., Gimond C., Rousselle P. Integrinmediated cellular interactions with laminins. The Laminins, P. Ekblom, R. Timpl. Harwood Academic Publishers. 1996; 127–158
   Google Scholar
• Aumailley M., Mann K., von der Mark H., Timpl 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
• Belkin A. M., Koteliansky V. E. Interaction of iodinated vinculin, metavinculin and α-actinin with cyto skeletal proteins. FEBS Lett. 1987; 220: 291–294
   PubMed Web of Science ®Google Scholar
• Brands R., Feltkamp C. A. Wet cleaving of cells: a method to introduce macromolecules into the cytoplasm. Application for immunolocalization of cytosol-exposed antigens. Exp. Cell Res. 1988; 176: 309–318
   PubMed Web of Science ®Google Scholar
• Brown M. C., Perrotta J. A., Turner C. E. Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding. J. Cell Biol. 1996; 135: 1109–1123
   PubMed Web of Science ®Google Scholar
• Burn P., Kupfer A., Singer S. Dynamic membrane-cytoskeletal interactions: specific association of integrin and talin arises in vivo after phorbol ester treatment of peripheral blood lymphocytes. Proc. Natl. Acad. Sci. USA 1988; 85: 497–501
   PubMed Web of Science ®Google Scholar
• Burridge K., Mangeat P. An interaction between vinculin and talin. Nature 1984; 308: 744–746
   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
• Chen H. C., Guan J. L. The association of focal adhesion kinase with a 200-kDa protein that is tyrosine phosphorylated in response to platelet-derived growth factor. Eur. J. Biochem. 1996; 235: 495–500
   PubMedGoogle Scholar
• Clark E. A., Brugge J. S. Integrins and signal transduction pathways: the road taken. Science 1995; 268: 233–238
   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 mobility 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
• Gilmore A. P., Wood C., Ohanian V., Jackson P, Patel B., Rees D. J.G., Hynes R. O., Critchley D. R. The cytoskeletal protein talin contains at least two distinct vinculin binding domains. J. Cell Biol. 1993; 122: 337–347
   PubMed Web of Science ®Google Scholar
• Gimond C., Mercier I., Weber I., Aumailley M. Cell adhesion complexes formed by OVCAR-4 cells on Jaminin-1 differ from those observed on fibronectin. Cell Adh. Comm. 1996; 3: 527–539
   PubMed Web of Science ®Google Scholar
• Hemmings L., Kuhlman P. A., Critchley D. R. Analysis of the actin-binding domain of α-actinin by mutagenesis and demonstration that dystrophin contains a functionally homologous domain. J. Cell Biol. 1992; 116: 1369–1380
   PubMed Web of Science ®Google Scholar
• Horwitz A., Duggan K., Buck C., Beckerle M. C., Burridge K. Interaction of plasma-membrane fibronectin receptor with talin - a transmembrane linkage. Nature 1986; 320: 531–533
   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
• Jockusch B. M., Isenberg G. Interaction of α-actinin and vinculin with actin: opposite effects on filament network formation. Proc. Natl. Acad. Sci. USA 1981; 78: 3005–3009
   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
• Luna E. J., Hitt A. L. Cytoskeleton-plasma membrane interactions. Science 1992; 258: 955–964
   PubMed Web of Science ®Google Scholar
• Mickka S. I., Ingham K. C., Menache D. Rapid methods for isolation of human plasma fibronectin. Thromb. Res. 1982; 27: 1–14
   PubMed Web of Science ®Google Scholar
• Muguruma M., Matsumura S., Fukazawa T. Augmentation of α-actinin induced gelation of actin by talin. J. Biol. Chem. 1992; 267: 5621–5624
   PubMed Web of Science ®Google Scholar
• Nermut M. V., Eason P., Hirst E. M., Kellie S. Cell/substratum adhesions in RSV-transformed rat fibroblasts. Exp. Cell Res. 1991; 193: 382–397
   PubMed Web of Science ®Google Scholar
• Otey C. A., Pavalko F. M., Burridge K. An interaction between α-actinin and the β1 integrin subunit in vitro. J. Cell Biol. 1990; 111: 721–729
   PubMed Web of Science ®Google Scholar
• Otey C. A., Vasquez G. B., Burridge K., Erickson B. W. Mapping of the α-actinin binding site within the β1 integrin cytoplasmic domain. J. Biol. Chem. 1993; 268: 21193–21197
   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
• Pavalko F. M., Burridge K. Disruption of the actin cytoskeleton after microinjection of proteolytic fragments of α-actinin. J. Cell Biol. 1991; 114: 481–491
   PubMed Web of Science ®Google 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
• 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
• Sato M., Schwartz W. H., Pollard T. D. Dependence of the mechanical properties of actin/α-actinin gels on deformation rate. Nature 1987; 325: 828–830
   PubMed Web of Science ®Google Scholar
• Schaller M. D., Otey C. A., Hildebrand J. D., Parsons J. T. Focal adhesion kinase and paxillin bind to peptides mimicking β integrin cytoplasmic domains. J. Cell Biol. 1995; 130: 1181–1187
   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
• Tachibana K., Sato T., D'Avitro N., Morimoto C. Direct association of pp125FAK with paxillin, the focal adhesion-targeting mechanism of pp125FAK. J. Exp. Med. 1995; 182: 1089–1099
   PubMed Web of Science ®Google Scholar
• Tapley P, Horwitz A., Buck C., Duggan K., Rohrschncider L. Integrins isolated from Rous sarcoma virus-transformed chicken embryo fibroblasts. Oncogens 1989; 4: 325–333
   PubMed Web of Science ®Google Scholar
• Tarone G., Cirillo D., Giancotti P. G., Comogho G. M., Marchisio P. M. Rous sarcoma virus-transformed fibroblasts adhere primarily at discrete protrusions of the ventral membrane called podosomes. Exp. Cell Res. 1985; 159: 141–157
   PubMed Web of Science ®Google Scholar
• Tawil N., Wilson P., Carbonetto S. Integrins in point contacts mediate cell spreading: factors that regulate integrin accumulation in point contacts vs. focal contacts. J. Cell Biol. 1993; 120: 261–271
   PubMed Web of Science ®Google Scholar
• Turner C. E., Glenney J. R., Burridge K. Paxillin a new vinculin-binding protein present in focal adhesions. J. Cell Biol. 1990; 111: 1059–1068
   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
• Wachsstock D. H., Wilkins J. A., Lin S. Specific interaction of vinculin with α-actinin. Biochent. Biophys. Res. Commun. 1987; 146: 554–560
   PubMed Web of Science ®Google Scholar
• Westmeyer A., Ruhnau K., Wegner A., Jockush B. Antibody mapping of functional domains in vinculin. EMBO J. 1990; 9: 2071–2078
   PubMed Web of Science ®Google Scholar
• Wilkins J. A., Risinger M. A., Coffez E., Lin S. Purification of a vinculin binding protein from smooth muscle. J. Cell Biol. 1987; 104: 130a
   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
• Yamada K. M., Geiger B. Molecular interactions in cell adhesion complexes. Curr. Op. Cell Biol. 1997; 9: 76–85
   PubMed Web of Science ®Google Scholar
• Zachary I., Rozengurt E. Focal adhesion kinase (p125FAK): a point convergence in the action of neuropeptides, integrins, and oncogenes. Cell 1992; 71: 891–894
   PubMed Web of Science ®Google Scholar