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A more recent version of this article appeared on June 1, 2003
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Submitted on July 3, 2002
Revised on February 8, 2003
Accepted on February 18, 2003
1 Department of Oncology, University of Alberta/Cross Cancer Institute, Edmonton Alberta, Canada T6G 1Z2
2 Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, PA
3 Department of Cell Biology, University of Alberta, Edmonton, Alberta, Canada T6G 1Z2
* Corresponding author. E-mail address: lpilarsk{at}gpu.srv.ualberta.ca.
RHAMM, an acidic coiled-coil protein, has previously been characterized as a cell surface receptor for hyaluronan, and a microtubule associated intracellular hyaluronan binding protein. In this study, we demonstrate that a subset of cellular RHAMM localizes to the centrosome and functions in the maintenance of spindle integrity. We confirm a previous study showing that the amino-terminus of RHAMM interacts with microtubules and further demonstrate that a separate carboxy-terminal domain is required for centrosomal targeting. This motif overlaps the defined hyaluronan binding domain and bears 72% identity to the dynein interaction domain of Xklp2. RHAMM antibodies coimmunprecipitate dynein intermediate chain from Xenopus and HeLa extracts. Deregulation of RHAMM expression inhibits mitotic progression and affects spindle architecture. Structure, localization and function, along with phylogenetic analysis, suggests that RHAMM may be a new member of the TACC family. Thus, we demonstrate a novel centrosomal localization and mitotic spindle stabilizing function for RHAMM. Moreover, we provide a potential mechanism for this function in that RHAMM may cross-link centrosomal microtubules, through a direct interaction with microtubules and an association with dynein.
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