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Vol. 9, Issue 3, 545-559, March 1998
Max Planck Institute for Biochemistry, D-82152 Martinsried, Germany
DdLim, a multi-domain member of the cysteine-rich family of LIM
domain proteins, was isolated from Dictyostelium cells
where it localizes in lamellipodia and at sites of membrane ruffling. The transcription and expression of DdLim are developmentally regulated, and the timing of its increased association with the actin
cytoskeleton coincides with the acquisition in starved cells of a
motile, chemotactic behavior. Vegetative cells that overexpress DdLim
contain large lamella and exhibit ruffling at the cortex. The high
frequency of large, multinucleated mutant cells found in suspension
culture suggests that excess DdLim interferes with cytokinesis. DdLim
was also identified as a protein in a Dictyostelium cell
lysate that associated indirectly, but in a guanosine
triphosphate-dependent manner, with a GST-rac1 fusion protein. The data
presented suggest that DdLim acts as an adapter protein at the
cytoskeleton-membrane interface where it is involved in a
receptor-mediated rac1-signaling pathway that leads to actin
polymerization in lamellipodia and ultimately cell motility.
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