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Max-Planck-Institut für Biochemie, D-82152 Martinsried, Germany
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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