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Vol. 10, Issue 1, 161-178, January 1999
Max-Planck-Institute for Biochemistry, D-82152 Martinsried, Germany
The molecular and functional characterization of a 125-kDa
Ca2+-extractable protein of the Triton X-100-insoluble
fraction of Dictyostelium cells identified a new type of
a gelsolin-related molecule. In addition to its five gelsolin segments,
this gelsolin-related protein of 125 kDa (GRP125) reveals a number of
unique domains, two of which are predicted to form coiled-coil regions.
Another distinct attribute of GRP125 concerns the lack of sequence
elements known to be essential for characteristic activities of
gelsolin-like proteins, i.e. the severing, capping, or nucleation of
actin filaments. The subcellular distribution of GRP125 to vesicular
compartments suggests an activity of GRP125 different from
actin-binding, gelsolin-related proteins. GRP125 expression is tightly
regulated and peaks at the transition to the multicellular
pseudoplasmodial stage of Dictyostelium development.
GRP125 was found indispensable for slug phototaxis, because slugs fail
to correctly readjust their orientation in the absence of GRP125.
Analysis of the GRP125-deficient mutant showed that GRP125 is required
for coupling photodetection to the locomotory machinery of slugs. We
propose that GRP125 is essential in the natural environment for the
propagation of Dictyostelium spores. We also present
evidence for further representatives of the GRP125 type in
Dictyostelium, as well as in heterologous cells from
lower to higher eukaryotes.
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