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Originally published as MBC in Press, 10.1091/mbc.E02-08-0516 on January 26, 2003
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Vol. 14, Issue 4, 1479-1488, April 2003

Accumulation of Cytoplasmic Dynein and Dynactin at Microtubule Plus Ends in Aspergillus nidulans Is Kinesin Dependent

Jun Zhang,* Shihe Li,* Reinhard Fischer,dagger and Xin Xiang*Dagger

 *Department of Biochemistry and Molecular Biology, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814; and  dagger Max-Planck-Institute for Terrestrial Microbiology, D-35043 Marburg, Germany

The mechanism(s) by which microtubule plus-end tracking proteins are targeted is unknown. In the filamentous fungus Aspergillus nidulans, both cytoplasmic dynein and NUDF, the homolog of the LIS1 protein, localize to microtubule plus ends as comet-like structures. Herein, we show that NUDM, the p150 subunit of dynactin, also forms dynamic comet-like structures at microtubule plus ends. By examining proteins tagged with green fluorescent protein in different loss-of-function mutants, we demonstrate that dynactin and cytoplasmic dynein require each other for microtubule plus-end accumulation, and the presence of cytoplasmic dynein is also important for NUDF's plus-end accumulation. Interestingly, deletion of NUDF increases the overall accumulation of dynein and dynactin at plus ends, suggesting that NUDF may facilitate minus-end-directed dynein movement. Finally, we demonstrate that a conventional kinesin, KINA, is required for the microtubule plus-end accumulation of cytoplasmic dynein and dynactin, but not of NUDF.

Online version of this article contains video material for some figures. Online version available at www.molbiolcell.org.

Dagger Corresponding author. E-mail address: xxiang{at}usuhs.mil.

Molecular Biology of the Cell
Vol. 14, 1479-1488, April 2003
Copyright © 2003 by The American Society for Cell Biology


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