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A more recent version of this article appeared on September 1, 2002
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Submitted on February 28, 2002
Revised on June 7, 2002
Accepted on June 14, 2002
-tubulin ring complex
1 Biosignal Research Center, Kobe University, Kobe 657-8501, Japan
2 Graduate School of Science and Technology, Kobe University, Kobe 657-8501, Japan
3 Biosignal Research Center, and Graduate School of Science and Technology, Kobe University, Kobe 657-8501, Japan
* Corresponding author. E-mail address: yonodayo{at}kobe-u.ac.jp.
Microtubule assembly is initiated by -tubulin ring complex (-TuRC). In yeast, microtubule is nucleated from -TuRC anchored to the amino terminus of the spindle pole body component Spc110p, which interacts with Cmd1p (calmodulin) at the carboxyl 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 shares high homology with the caroboxyl-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 each other, and with endogenous GCP2 and -tubulin, suggesting that CG-NAP and kendrin form complex 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, combination of these antibodies resulted in stronger inhibition. These results implicate that CG-NAP and kendrin provide sites for microtubule nucleation in mammalian centrosome by anchoring -TuRC.
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