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MBC in Press, published online ahead of print November 17, 2004
Mol. Biol. Cell 10.1091/mbc.E04-08-0682

A more recent version of this article appeared on February 1, 2005
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Submitted on August 9, 2004
Revised on October 6, 2004
Accepted on October 31, 2004

The C. elegans Aurora B Kinase AIR-2 Phosphorylates and Is Required for the Localization of a BimC Kinesin to Meiotic and Mitotic Spindles

John D. Bishop,*{dagger} Zhenbo Han,* and Jill M. Schumacher{ddagger}{sect}

*Department of Molecular Genetics, The University of Texas M. D. Anderson Cancer Center, Houston, TX 77030; {ddagger}Genes and Development Program, Graduate School of Biomedical Sciences, The University of Texas-Houston, Houston, TX 77030

Monitoring Editor: Susan Strome

BimC kinesins are required for mitotic spindle assembly in a variety of organisms. These proteins are localized to centrosomes, spindle microtubules, and the spindle midzone. We have previously shown that the C. elegans Aurora B kinase AIR-2 is required for the localization of the ZEN-4 kinesin protein to midzone microtubules. To determine whether the association of BimC kinesins with spindle microtubules is also dependent on AIR-2, we examined the expression pattern of BMK-1, a C. elegans BimC kinesin, in wild-type and AIR-2-deficient embryos. BMK-1 is highly expressed in the hermaphrodite gonad and is localized to meiotic spindle microtubules in the newly fertilized embryo. In mitotic embryos, BMK-1 is associated with spindle microtubules from prophase through anaphase, and is concentrated at the spindle midzone during anaphase and telophase. In the absence of AIR-2, BMK-1 localization to meiotic and mitotic spindles is greatly reduced. This is not consequence of loss of ZEN-4 localization as BMK-1 is appropriately localized in ZEN-4 deficient embryos. Furthermore, AIR-2 and BMK-1 directly interact with one another and the C-terminal tail domain of BMK-1 is specifically phosphorylated by AIR-2 in vitro. Together with our previous data, these results suggest that at least one function of the Aurora B kinases is to recruit spindle-associated motor proteins to their sites of action.


{dagger}Present Address: Invitrogen Corporation, 1600 Faraday Ave., PO Box 6482, Carlsbad, CA 92008.

{sect}Corresponding author. E-mail: jschumac{at}mdanderson.org







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