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Originally published as MBC in Press, 10.1091/mbc.E04-08-0682 on November 17, 2004

Vol. 16, Issue 2, 742-756, February 2005

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The Caenorhabditis elegans Aurora B Kinase AIR-2 Phosphorylates and Is Required for the Localization of a BimC Kinesin to Meiotic and Mitotic Spindles{boxd}

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

* 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

Submitted August 9, 2004; Revised October 6, 2004; Accepted October 31, 2004
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 Caenorhabditis 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 a consequence of loss of ZEN-4 localization because 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.


Article published online ahead of print in MBC in Press on November 17, 2004 (http://www.molbiolcell.org/cgi/doi/10.1091/mbc.E04-08-0682).

{boxd} The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

{dagger} Present address: Invitrogen, 1600 Faraday Ave., P.O. Box 6482, Carlsbad, CA 92008.

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




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