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Vol. 13, Issue 9, 3235-3245, September 2002

Centrosomal Proteins CG-NAP and Kendrin Provide Microtubule Nucleation Sites by Anchoring -Tubulin Ring Complex

Mikiko Takahashi,^* Akiko Yamagiwa, Tamako Nishimura, Hideyuki Mukai,^* and Yoshitaka Ono^*

 ^*Biosignal Research Center and  Graduate School of Science and Technology, Kobe University, Kobe 657-8501, Japan

Microtubule assembly is initiated by the -tubulin ring complex (-TuRC). In yeast, the microtubule is nucleated from -TuRC anchored to the amino-terminus of the spindle pole body component Spc110p, which interacts with calmodulin (Cmd1p) at the carboxy-terminus. However, mammalian protein that anchors -TuRC remains to be elucidated. A giant coiled-coil protein, CG-NAP (centrosome and Golgi localized PKN-associated protein), was localized to the centrosome via the carboxyl-terminal region. This region was found to interact with calmodulin by yeast two-hybrid screening, and it shares high homology with the carboxyl-terminal region of another centrosomal coiled-coil protein, kendrin. The amino-terminal region of either CG-NAP or kendrin indirectly associated with -tubulin through binding with -tubulin complex protein 2 (GCP2) and/or GCP3. Furthermore, endogenous CG-NAP and kendrin were coimmunoprecipitated with each other and with endogenous GCP2 and -tubulin, suggesting that CG-NAP and kendrin form complexes and interact with -TuRC in vivo. These proteins were localized to the center of microtubule asters nucleated from isolated centrosomes. Pretreatment of the centrosomes by antibody to CG-NAP or kendrin moderately inhibited the microtubule nucleation; moreover, the combination of these antibodies resulted in stronger inhibition. These results imply that CG-NAP and kendrin provide sites for microtubule nucleation in the mammalian centrosome by anchoring -TuRC.

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Corresponding author. E-mail address: yonodayo{at}kobe-u.ac.jp.

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Molecular Biology of the Cell
Vol. 13, 3235-3245, September 2002
Copyright © 2002 by The American Society for Cell Biology

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