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Vol. 15, Issue 1, 219-233, January 2004
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University of California Davis, Davis, California 95616
Submitted July 11, 2003;
Revised September 2, 2003;
Accepted September 3, 2003
Monitoring Editor: Lawrence Goldstein
Mitosis requires the concerted activities of multiple microtubule (MT)-based motor proteins. Here we examined the contribution of the chromokinesin, KLP3A, to mitotic spindle morphogenesis and chromosome movements in Drosophila embryos and cultured S2 cells. By immunofluorescence, KLP3A associates with nonfibrous punctae that concentrate in nuclei and display MT-dependent associations with spindles. These punctae concentrate in indistinct domains associated with chromosomes and central spindles and form distinct bands associated with telophase midbodies. The functional disruption of KLP3A by antibodies or dominant negative proteins in embryos, or by RNA interference (RNAi) in S2 cells, does not block mitosis but produces defects in mitotic spindles. Time-lapse confocal observations of mitosis in living embryos reveal that KLP3A inhibition disrupts the organization of interpolar (ip) MTs and produces short spindles. Kinetic analysis suggests that KLP3A contributes to spindle pole separation during the prometaphase-to-metaphase transition (when it antagonizes Ncd) and anaphase B, to normal rates of chromatid motility during anaphase A, and to the proper spacing of daughter nuclei during telophase. We propose that KLP3A acts on MTs associated with chromosome arms and the central spindle to organize ipMT bundles, to drive spindle pole separation and to facilitate chromatid motility.
Abbreviations used: KLP3A, kinesin-like-protein at 3A; MTs, microtubules; ipMTs, interpolar MTs; GST, glutathione-S-transferase; NEB, nuclear envelope breakdown; kMTs, kinetochore MTs; MMAP, microtubule- and microfilament-associated protein.
Online version of this article contains supplementary figures, tables, and videos for some figures. Online version is available at www.molbiolcell.org.
* Present address: Albert Einstein College of Medicine, Department of Physiology and Biophysics, 1300 Morris Park Avenue, Bronx, NY 10461-1602.
Corresponding author. E-mail address: jmscholey{at}ucdavis.edu.
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