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MBC in Press, published online ahead of print September 22, 2004
Mol. Biol. Cell 10.1091/mbc.E04-05-0385

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Submitted on May 11, 2004
Accepted on September 13, 2004

Characterization of the Tpx2 Domains Involved in Microtubule Nucleation and Spindle Assembly in Xenopus Egg Extracts

Stéphane Brunet,* Teresa Sardon, Timo Zimmerman, Torsten Wittmann,{dagger} Rainer Pepperkok, Eric Karsenti, and Isabelle Vernos{ddagger}

Cell Biology and Biophysics Program, EMBL, Heidelberg 69 117, Germany

Monitoring Editor: Lawrence Goldstein

TPX2 has multiple functions during mitosis including microtubule nucleation around the chromosomes and the targeting of Xklp2 and Aurora A to the spindle. We have performed a detailed domain functional analysis of TPX2 and found that a large N-terminal domain containing the Aurora A binding peptide interacts directly with and nucleates microtubules in pure tubulin solutions. However, it cannot substitute the endogenous TPX2 to support microtubule nucleation in response to Ran GTP and spindle assembly in egg extracts. By contrast, a large C-terminal domain of TPX2 that does not bind directly to pure microtubules and does not bind Aurora A kinase rescues microtubule nucleation in response to Ran-GTP and spindle assembly in TPX2 depleted extract. These and previous results suggest that under physiological conditions, TPX2 is essential for microtubule nucleation around chromatin and functions in a network of other molecules some of which also regulated by RanGTP.

Present addresses: *Laboratoire de Biochimie Cellulaire CNRS UMR 7098, bat C-Case 265, 9 Quai St Bernard, 75252 Paris Cedex 05, France; {dagger}Department of Cell Biology and Institute for Childhood and Neglected Diseases, The Scripps Research Institute, La Jolla, CA 92037.

{ddagger}Corresponding author. E-mail: vernos{at}embl-heidelberg.de






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