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Vol. 13, Issue 3, 965-977, March 2002
Max-Planck-Institut für terrestrische Mikrobiologie,
Karl-von-Frisch-Straße, D-35043 Marburg, Germany
The endoplasmic reticulum (ER) of most vertebrate cells is spread
out by kinesin-dependent transport along microtubules, whereas studies
in Saccharomyces cerevisiae indicated that motility of fungal ER is an actin-based process. However, microtubules are of minor
importance for organelle transport in yeast, but they are crucial for
intracellular transport within numerous other fungi. Herein, we set out
to elucidate the role of the tubulin cytoskeleton in ER organization
and dynamics in the fungal pathogen Ustilago maydis. An
ER-resident green fluorescent protein (GFP)-fusion protein localized to
a peripheral network and the nuclear envelope. Tubules and patches
within the network exhibited rapid dynein-driven motion along
microtubules, whereas conventional kinesin did not participate in ER
motility. Cortical ER organization was independent of microtubules or
F-actin, but reformation of the network after experimental disruption
was mediated by microtubules and dynein. In addition, a polar gradient
of motile ER-GFP stained dots was detected that accumulated around the
apical Golgi apparatus. Both the gradient and the Golgi apparatus were
sensitive to brefeldin A or benomyl treatment, suggesting that the
gradient represents microtubule-dependent vesicle trafficking between
ER and Golgi. Our results demonstrate a role of cytoplasmic dynein and
microtubules in motility, but not peripheral localization of the ER in
U. maydis.
Corresponding author. E-mail address:
gero.steinberg{at}mailer.uni-marburg.de.
Online version of this article contains video
material for some figures. Online version available at
www.molbiolcell.org.
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