HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE ADVANCED SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Nishimura, T. Articles by Ono, Y. Search for Related Content PubMed PubMed Citation Articles by Nishimura, T. Articles by Ono, Y.

¹ Graduate School of Science and Technology,
² Biosignal Research Centre, Kobe University, Kobe 657-8501, Japan

Centrosome duplication occurs once per cell cycle and is thought to be triggered by cyclin E-cdk2. However, it is largely unknown how the duplication is regulated. Here, we found that the expression of the centrosome-targeting region of CG-NAP (centrosome and Golgi-localized PKN-associated protein), which we designate as CG-NAP/D, increased the number of centrosomes in Chinese hamster ovary (CHO)-K1 cells. The amplified centrosomes co-localized with centrosome markers -tubulin, centrin-2 and kendrin as well as endogenous CG-NAP. When CG-NAP/D was dislocated from centrosomes by deleting the centrosome-targeting domain or by fusing with a membrane-targeting sequence, centrosome amplification was suppressed. CG-NAP/D interacted with exogenously expressed cyclin E, which co-localized at centrosomes. The immunoprecipitates of CG-NAP/D exhibited histone H1 kinase activity, suggesting the co-immunoprecipitation of active cyclin-cdk complexes. Furthermore, centrosome fractions prepared from cells expressing CG-NAP/D contained increased amount of cdk2 compared with those from control cells. Centrosome amplification by CG-NAP/D was suppressed by co-expression of a mutant cyclin E unable to interact with cdk2. These results suggest that CG-NAP/D causes centrosome amplification by anchoring excess amount of cyclin E-cdk2 to centrosomes and, possibly, CG-NAP participates in centrosome duplication by recruiting cyclin E-cdk2 to centrosomes in normal cell cycle.

^* Correspondence: E-mail: yonodayo{at}kobe-u.ac.jp

This article has been cited by other articles:

				C. L. Nguyen, C. Eichwald, M. L. Nibert, and K. Munger Human Papillomavirus Type 16 E7 Oncoprotein Associates with the Centrosomal Component {gamma}-Tubulin J. Virol., December 15, 2007; 81(24): 13533 - 13543. [Abstract] [Full Text] [PDF]

				N. T. Chartier, C. I. Oddou, M. G. Laine, B. Ducarouge, C. A. Marie, M. R. Block, and M. R. Jacquier-Sarlin Cyclin-Dependent Kinase 2/Cyclin E Complex Is Involved in p120 Catenin (p120ctn) Dependent Cell Growth Control: A New Role for p120ctn in Cancer Cancer Res., October 15, 2007; 67(20): 9781 - 9790. [Abstract] [Full Text] [PDF]

				H.-S. Kim, M. Takahashi, K. Matsuo, and Y. Ono Recruitment of CG-NAP to the Golgi apparatus through interaction with dynein-dynactin complex Genes Cells, March 1, 2007; 12(3): 421 - 434. [Abstract] [Full Text] [PDF]

				C. Sutterlin, R. Polishchuk, M. Pecot, and V. Malhotra The Golgi-associated Protein GRASP65 Regulates Spindle Dynamics and Is Essential for Cell Division Mol. Biol. Cell, July 1, 2005; 16(7): 3211 - 3222. [Abstract] [Full Text] [PDF]