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A more recent version of this article appeared on April 1, 2006
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Submitted on November 28, 2005
Revised on January 25, 2006
Accepted on January 31, 2006
*Department of Pharmacology, UMDNJ-Robert Wood Johnson Medical School, Piscataway, NJ 08854; Department of Biochemistry and Molecular Biology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814
Monitoring Editor: Kerry Bloom
Proteins in the cytoplasmic dynein pathway accumulate at the microtubule plus end, giving the appearance of comets when observed in live cells. The targeting mechanism for NUDF (LIS1/Pac1) of Aspergillus nidulans, a key component of the dynein pathway, has not been clear. Previous studies have demonstrated NUDF/LIS1/Pac1’s physical interactions with both NUDE/NUDEL/Ndl1 and CLIP-170/Bik1. Here we have identified the A. nidulans CLIP-170 homolog, CLIPA. The clipA deletion did not cause an obvious nuclear distribution phenotype but affected cytoplasmic microtubules in an unexpected manner. Although more microtubules failed to undergo long-range growth toward the hyphal tip at 32°C, those that reached the hyphal tip were less likely to undergo catastrophe. Thus, in addition to acting as a growth-promoting factor, CLIPA also promotes microtubule dynamics. In the absence of CLIPA, GFP-labeled cytoplasmic dynein heavy chain, p150Glued dynactin and NUDF were all seen as plus-end comets at 32°C. However, under the same conditions, deletion of both clipA and nudE almost completely abolished NUDF comets although nudE deletion itself did not cause a dramatic change in NUDF localization. Based on these results, we suggest that CLIPA and NUDE both recruit NUDF to the microtubule plus end. The plus-end localization of CLIPA itself seems to be regulated by different mechanisms under different physiological conditions. While the KipA kinesin (Kip2/Tea2 homolog) did not affect CLIPA’s plus-end localization at 32°C, it was required for enhancing CLIPA’s plus-end accumulation at an elevated temperature (42°C).
These authors contributed equally to this work.
Address correspondence to:
Xin Xiang (xxiang{at}usuhs.mil)
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