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Vol. 10, Issue 11, 3717-3728, November 1999
and
*Department of Biology, Indiana University, Bloomington, Indiana
47405-6801; In axons, organelles move away from (anterograde) and toward
(retrograde) the cell body along microtubules. Previous studies have
provided compelling evidence that conventional kinesin is a major motor
for anterograde fast axonal transport. It is reasonable to expect that
cytoplasmic dynein is a fast retrograde motor, but relatively few tests
of dynein function have been reported with neurons of intact organisms.
In extruded axoplasm, antibody disruption of kinesin or the dynactin
complex (a dynein activator) inhibits both retrograde and anterograde
transport. We have tested the functions of the cytoplasmic dynein heavy
chain (cDhc64C) and the p150Glued
(Glued) component of the dynactin complex with the use
of genetic techniques in Drosophila.
cDhc64C and Glued mutations disrupt fast
organelle transport in both directions. The mutant phenotypes, larval
posterior paralysis and axonal swellings filled with retrograde and
anterograde cargoes, were similar to those caused by kinesin mutations.
Why do specific disruptions of unidirectional motor systems cause
bidirectional defects? Direct protein interactions of kinesin with
dynein heavy chain and p150Glued were not detected.
However, strong dominant genetic interactions between kinesin, dynein,
and dynactin complex mutations in axonal transport were observed. The
genetic interactions between kinesin and either Glued or
cDhc64C mutations were stronger than those between
Glued and cDhc64C mutations themselves.
The shared bidirectional disruption phenotypes and the dominant genetic
interactions demonstrate that cytoplasmic dynein, the dynactin complex,
and conventional kinesin are interdependent in fast axonal transport.
Department of Genetics and Cell Biology,
University of Minnesota, St. Paul, Minnesota 55108-1095; and
§Department of Biology, University of Massachusetts,
Boston, Massachusetts 02125
Corresponding author. E-mail address:
mamartin{at}bio.indiana.edu.
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