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J. Cell Biol.,
Volume 140, Number 4, February 23, 1998 897-910
Department of Biology, Washington University, St. Louis, Missouri 63130
Abstract. Coordination of cellular organization requires the interaction of the cytoskeletal filament systems. Recently, several lines of investigation have suggested that transport of cellular components along both
microtubules and actin filaments is important for cellular organization and function. We report here on molecules that may mediate coordination between the actin
and microtubule cytoskeletons. We have identified a
195-kD protein that coimmunoprecipitates with a class
VI myosin, Drosophila 95F unconventional myosin. Cloning and sequencing of the gene encoding the
195-kD protein reveals that it is the first homologue
identified of cytoplasmic linker protein (CLIP)-170, a
protein that links endocytic vesicles to microtubules.
We have named this protein D-CLIP-190 (the predicted molecular mass is 189 kD) based on its similarity
to CLIP-170 and its ability to cosediment with microtubules. The similarity between D-CLIP-190 and CLIP-170 extends throughout the length of the proteins, and
they have a number of predicted sequence and structural features in common. 95F myosin and D-CLIP-190
are coexpressed in a number of tissues during embryogenesis in Drosophila. In the axonal processes of neurons, they are colocalized in the same particulate
structures, which resemble vesicles. They are also colocalized at the posterior pole of the early embryo, and this localization is dependent on the actin cytoskeleton.
The association of a myosin and a homologue of a microtubule-binding protein in the nervous system and at
the posterior pole, where both microtubule and actin-dependent processes are known to be important, leads
us to speculate that these two proteins may functionally link the actin and microtubule cytoskeletons.
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