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MBC in Press, published online ahead of print November 28, 2005
Mol. Biol. Cell 10.1091/mbc.E05-08-0810

A more recent version of this article appeared on February 1, 2006
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Submitted on August 29, 2005
Revised on October 20, 2005
Accepted on November 10, 2005

A Complex of Two Centrosomal Proteins, CAP350 and FOP, Cooperates with EB1 in MT Anchoring

Xiumin Yan, Robert Habedanck, and Erich A. Nigg

Department of Cell Biology, Max-Planck-Institute of Biochemistry, D-82152 Martinsried, Germany

Monitoring Editor: Yixian Zheng

The anchoring of microtubules (MTs) to subcellular structures is critical for cell shape, polarity and motility. In mammalian cells, the centrosome is a prominent MT anchoring structure. A number of proteins, including ninein, p150Glued and EB1, have been implicated in centrosomal MT anchoring, but the process is far from understood. Here we show that CAP350 and FOP (FGFR1 oncogene partner) form a centrosomal complex required for MT anchoring. We show that the C-terminal domain of CAP350 interacts directly with FOP and that both proteins localize to the centrosome throughout the cell cycle. FOP also binds to EB1 and is required for localizing EB1 to the centrosome. Depletion of either CAP350, FOP or EB1 by siRNA causes loss of MT anchoring and profound disorganization of the MT network. These results have implications for the mechanisms underlying MT anchoring at the centrosome and they attribute a key MT anchoring function to two novel centrosomal proteins, CAP350 and FOP.


Address correspondence to: Erich A. Nigg (nigg{at}biochem.mpg.de)




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