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A more recent version of this article appeared on March 1, 2002
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Submitted on September 26, 2001
Revised on November 16, 2001
Accepted on December 4, 2001
1 Max-Planck-Institut für terrestrische Mikrobiologie, Karl-von-Frisch-Strabe, D-35043 Marburg, Germany
2 Max-Planck-Institut für terrestrische Mikrobiologie, Karl-von-Frisch-Strabe, D-35043 Marburg, Germany (present address: Institute for Cell Biology, LMU, Schillerstr. 42, 80336 Munich, Germany)
* Corresponding author. E-mail address: Gero.Steinberg{at}mailer.uni-marburg.de.
The endoplasmic reticulum (ER) of most vertebrate cells is spread out by kinesin-dependent transport along microtubules, while studies in S. 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. Here we set out to elucidate the role of the tubulin cytoskeleton in ER organization and dynamics in the fungal pathogen U. maydis. An ER-resident 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, while 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 vesicles 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.
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