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Vol. 16, Issue 6, 3064-3076, June 2005
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* Marine Biological Laboratory, Woods Hole, MA 02543;
Department of Systems Biology, Harvard Medical School, Boston, MA 02115;
Department of Biology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599;
Laboratory of Chemistry and Cell Biology, Rockefeller University, New York, NY 10021; and
|| Department of Cellular and Molecular Medicine, University of California–San Diego, San Diego, CA 92093-0685
Submitted March 1, 2005;
Accepted March 14, 2005
Monitoring Editor: Tim Stearns
Metaphase spindles assemble to a steady state in length by mechanisms that involve microtubule dynamics and motor proteins, but they are incompletely understood. We found that Xenopus extract spindles recapitulate the length of egg meiosis II spindles, by using mechanisms intrinsic to the spindle. To probe these mechanisms, we perturbed microtubule polymerization dynamics and opposed motor proteins and measured effects on spindle morphology and dynamics. Microtubules were stabilized by hexylene glycol and inhibition of the catastrophe factor mitotic centromere-associated kinesin (MCAK) (a kinesin 13, previously called XKCM) and destabilized by depolymerizing drugs. The opposed motors Eg5 and dynein were inhibited separately and together. Our results are consistent with important roles for polymerization dynamics in regulating spindle length, and for opposed motors in regulating the relative stability of bipolar versus monopolar organization. The response to microtubule destabilization suggests that an unidentified tensile element acts in parallel with these conventional factors, generating spindle shortening force.
The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).
Address correspondence to: T. J. Mitchison (timothy_mitchison{at}hms.harvard.edu).
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