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Human Molecular Genetics Advance Access originally published online on October 3, 2005
Human Molecular Genetics 2005 14(21):3113-3128; doi:10.1093/hmg/ddi339
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© The Author 2005. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Recruitment of katanin p60 by phosphorylated NDEL1, an LIS1 interacting protein, is essential for mitotic cell division and neuronal migration

Kazuhito Toyo-Oka1, Shinji Sasaki2,{dagger}, Yoshihisa Yano1, Daisuke Mori1, Takuya Kobayashi3, Yoko Y. Toyoshima3, Suzumi M. Tokuoka4, Satoshi Ishii4, Takao Shimizu4, Masami Muramatsu2, Noriko Hiraiwa5, Atsushi Yoshiki5, Anthony Wynshaw-Boris6 and Shinji Hirotsune1,2,*

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

* To whom correspondence should be addressed. Tel: +6 66453725; Fax: +6 66453727; Email: shinjih{at}med.osaka-cu.ac.jp

Received July 19, 2005; Accepted September 7, 2005

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.

{dagger} Present address: Department of Anatomy, Keio University School of Medicine, 35 Shinanomachi, Shinjuku-ku, Tokyo 160-8582, Japan.


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