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MBC in Press, published online ahead of print January 26, 2003
Mol. Biol. Cell 10.1091/mbc.E02-08-0516

A more recent version of this article appeared on April 1, 2003
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Submitted on August 19, 2002
Revised on October 28, 2002
Accepted on December 4, 2002

The accumulation of cytoplasmic dynein and dynactin at microtubule plus-ends in Aspergillus nidulans is kinesin dependent

Jun Zhang1, Shihe Li1, Reinhard Fischer2, and Xin Xiang1*

1 Department of Biochemistry, Uniformed Services University of the Health Sciences, Bethesda, MD 20814, U.S.A.
2 Max-Planck-Institute for Terrestrial Microbiology, Karl-von-Frisch-Str., D-35043 Marburg, Germany

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

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. Here we show that NUDM, the p150 subunit of dynactin, also forms dynamic comet-like structures at microtubule plus ends. By examining GFP-fusion proteins 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.




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