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First published online 29 May 2007
doi: 10.1242/jcs.03458

Journal of Cell Science 120, 2106-2116 (2007)
Published by The Company of Biologists 2007
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Research Article

Characterization of NIP2/centrobin, a novel substrate of Nek2, and its potential role in microtubule stabilization

Yeontae Jeong, Jungmin Lee, Kyeongmi Kim, Jae Cheal Yoo and Kunsoo Rhee*

Department of Biological Sciences and Research Center for Functional Cellulomics, Seoul National University, Seoul 151-742, Korea

* Author for correspondence (e-mail: rheek{at}snu.ac.kr)

Accepted 11 April 2007

Nek2 is a mitotic kinase whose activity varies during the cell cycle. It is well known that Nek2 is involved in centrosome splitting, and a number of studies have indicated that Nek2 is crucial for maintaining the integrity of centrosomal structure and microtubule nucleation activity. In the present study, we report that NIP2, previously identified as centrobin, is a novel substrate of Nek2. NIP2 was daughter-centriole-specific, but was also found in association with a stable microtubule network of cytoplasm. Ectopic NIP2 formed aggregates but was dissolved by Nek2 into small pieces and eventually associated with microtubules. Knockdown of NIP2 showed significant reduction of microtubule organizing activity, cell shrinkage, defects in spindle assembly and abnormal nuclear morphology. Based on our results, we propose that NIP2 has a role in stabilizing the microtubule structure. Phosphorylation may be crucial for mobilization of the protein to a new microtubule and stabilizing it.

Key words: NIP2, Centrobin, Nek2, Centrosome, Mitosis, Microtubule


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This article has been cited by other articles:


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J. Rapley, M. Nicolas, A. Groen, L. Regue, M. T. Bertran, C. Caelles, J. Avruch, and J. Roig
The NIMA-family kinase Nek6 phosphorylates the kinesin Eg5 at a novel site necessary for mitotic spindle formation
J. Cell Sci., December 1, 2008; 121(23): 3912 - 3921.
[Abstract] [Full Text] [PDF]


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