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Human Molecular Genetics Advance Access published online on October 3, 2005
Human Molecular Genetics, doi:10.1093/hmg/ddi339
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© The Author 2005. Published by Oxford University Press. All rights reserved
Received July 19, 2005
Accepted September 5, 2005

Article

Recruitment of Katanin P60 by Phosphorylated NDEL1, a LIS1 interacting protein, is Essential for Mitotic Cell Division and Neuronal Migration

Kazuhito Toyo-oka 1, Shinji Sasaki 2, Yoshihisa Yano 1, Daisuke Mori 1, Takuya Kobayashi 3, Yoko Y. Toyoshima 3, Suzumi M. Tokuoka 4, Satoshi Ishii 4, Takao Shimizu 4, Masami Muramatsu 2, Noriko Hiraiwa 5, Atsushi Yoshiki 5, Anthony Wynshaw-Boris 6, and Shinji Hirotsune 7*

1 Department of Genetic Disease Research, Osaka City University Graduate School of Medicine, Asahi-machi 1-4-3 Abeno, Osaka 545-8586, Japan
2 Division of Neuro-Science, Research Center for Genomic Medicine, Saitama Medical School Yamane 1397-1, Hidaka City Saitama 350-1241 Japan
3 Department of Life Sciences, Graduate School of Arts and Sciences, The University of Tokyo, 3-8-1 Komaba, Meguro-ku, Tokyo, 153-8902, Japan
4 Department of Biochemistry and Molecular Biology, Faculty of Medicine, The University of Tokyo , 7-3-1, Bunkyo-ku, Hongo, Tokyo 113-0033, Japan
5 Experimental Animal Division, Department of Biological Systems, BioResource Center, RIKEN Tsukuba Institute, 3-1-1 Koyadai, Tsukuba, Ibaraki 305-0074, Japan
6 Center for Human Genetics and Genomics, Departments of Pediatrics and Medicine, University of California, San Diego School of Medicine, 9500 Gilman Drive, Mailstop 0627 La Jolla, CA 92093-0627
7 Department of Genetic Disease Research, Osaka City University Graduate School of Medicine, Asahi-machi 1-4-3 Abeno, Osaka 545-8586, Japan; Division of Neuro-Science, Research Center for Genomic Medicine, Saitama Medical School Yamane 1397-1, Hidaka City Saitama 350-1241 Japan

* To whom correspondence should be addressed.
Shinji Hirotsune, E-mail: shinjih{at}med.osaka-cu.ac.jp


  Abstract

LIS1 is mutated in the human neuronal migration defect lissencephaly, and along with NDEL1 (formerly NUDEL), participates in the regulation of cytoplasmic dynein function during neuronal development. Targeted disruption of Ndel1 suggested that NDEL1 could have other molecular targets that regulate microtubule organization for proper neuronal migration. To further understanding the molecular mechanism of LIS1 and lissencephaly, we identified the katanin p60 microtubule severing protein as an additional molecular target of NDEL1. We demonstrate that phosphorylation of NDEL1 by Cdk5 facilitates interaction between NDEL1 and p60, suggesting that P-NDEL1 regulates the distribution of katanin p60. Abnormal accumulation of p60 in nucleus of Ndel1 null mutants supports an essential role of NDEL1 in p60 regulation. Complete loss of NDEL1 or expression of dominant negative mutants of p60 in migrating neurons results in defective migration and elongation of nuclear-centrosomal distance. Our results suggest that NDEL1 is essential for mitotic cell division and neuronal migration not only via regulation of cytoplasmic dynein function but also by modulation of katanin p60 localization and function.


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