The Journal of Cell Biology · 1997 · 144 citations · 64 references
Life SciencesCell BiologyMolecular BiologyCell AdhesionCytoskeletonEndocytosisActin FilamentsActin PolymerizationCell-cell AdhesionCytoskeletal LinkageActin-cytoskeleton CouplingAdhesion To SubstrateCell Surface GlycoproteinsCell-substrate AdhesionCell-substrate InteractionsGene Replacement ConstructsImpaired Cell AdhesionSubstrate Adhesion
Dictyostelium discoideum contains a full-length homologue of talin, a protein implicated in linkage of the actin system to sites of cell-to-substrate adhesion in fibroblasts and neuronal growth cones. Gene replacement eliminated the talin homologue in Dictyostelium and led to defects in phagocytosis and cell-to-substrate interaction of moving cells, two processes dependent on a continuous cross talk between the cell surface and underlying cytoskeleton. The uptake rate of yeast particles was reduced, and only bacteria devoid of the carbohydrate moiety of cell surface lipopolysaccharides were adhesive enough to be recruited by talin-null cells in suspension and phagocytosed. Cell-to-cell adhesion of undeveloped cells was strongly impaired in the absence of talin, in contrast with the cohesion of aggregating cells mediated by the phospholipid-anchored contact site A glycoprotein, which proved to be less talin dependent. The mutant cells were still capable of moving and responding to a chemoattractant, although they attached only loosely to a substrate via small areas of their surface. With their high proportion of binucleated cells, the talin-null mutants revealed interactions of the mitotic apparatus with the cell cortex that were not obvious in mononucleated cells.
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Interaction of plasma membrane fibronectin receptor with talin—a transmembrane linkage
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An interaction between vinculin and talin
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