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Published online April 23, 2007
doi:10.1083/jcb.200612011
The Journal of Cell Biology, Vol. 177, No. 2, 231-242
The Rockefeller University Press, 0021-9525 $30.00
© 2007 Zhang et al.
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Article

 Three microtubule severing enzymes contribute to the "Pacman-flux" machinery that moves chromosomes

Dong Zhang1, Gregory C. Rogers1,2, Daniel W. Buster1, and David J. Sharp1

1 Department of Physiology and Biophysics, Albert Einstein College of Medicine, Bronx, NY 10461
2 Department of Biology, University of North Carolina, Chapel Hill, NC 27599

Correspondence to David J. Sharp: dsharp{at}aecom.yu.edu

Chromosomes move toward mitotic spindle poles by a Pacman-flux mechanism linked to microtubule depolymerization: chromosomes actively depolymerize attached microtubule plus ends (Pacman) while being reeled in to spindle poles by the continual poleward flow of tubulin subunits driven by minus-end depolymerization (flux). We report that Pacman-flux in Drosophila melanogaster incorporates the activities of three different microtubule severing enzymes, Spastin, Fidgetin, and Katanin. Spastin and Fidgetin are utilized to stimulate microtubule minus-end depolymerization and flux. Both proteins concentrate at centrosomes, where they catalyze the turnover of {gamma}-tubulin, consistent with the hypothesis that they exert their influence by releasing stabilizing {gamma}-tubulin ring complexes from minus ends. In contrast, Katanin appears to function primarily on anaphase chromosomes, where it stimulates microtubule plus-end depolymerization and Pacman-based chromatid motility. Collectively, these findings reveal novel and significant roles for microtubule severing within the spindle and broaden our understanding of the molecular machinery used to move chromosomes.

Abbreviations used in this paper: ds, double-stranded; {gamma}-TuRC, {gamma}-tubulin ring complex; MT, microtubule.


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