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The Journal of Neuroscience, January 3, 2007, 27(1):15-26; doi:10.1523/JNEUROSCI.3826-06.2006

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Development/Plasticity/Repair
DISC1 Regulates the Transport of the NUDEL/LIS1/14-3-3 Complex through Kinesin-1

Shinichiro Taya,¹ Tomoyasu Shinoda,¹ Daisuke Tsuboi,¹ Junko Asaki,¹ Kumiko Nagai,¹ Takao Hikita,¹ Setsuko Kuroda,¹ Keisuke Kuroda,¹ Mariko Shimizu,¹ Shinji Hirotsune,² Akihiro Iwamatsu,³ and Kozo Kaibuchi¹

¹Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, 65 Tsurumai, Showa, Nagoya 466-8550, Japan, ²Department of Genetic Disease Research, Graduate School of Medicine, Osaka City University, Abeno, Osaka 545-8585, Japan, and ³Protein Research Network, Yokohama 236-0004, Japan

Correspondence should be addressed to Dr. Kozo Kaibuchi, Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, 65 Tsurumai, Showa, Nagoya 466-8550, Japan. Email: kaibuchi{at}med.nagoya-u.ac.jp

Disrupted-In-Schizophrenia 1 (DISC1) is a candidate gene for susceptibility to schizophrenia. DISC1 is reported to interact with NudE-like (NUDEL), which forms a complex with lissencephaly-1 (LIS1) and 14-3-3. 14-3-3 is involved in the proper localization of NUDEL and LIS1 in axons. Although the functional significance of this complex in neuronal development has been reported, the transport mechanism of the complex into axons and their functions in axon formation remain essentially unknown. Here we report that Kinesin-1, a motor protein of anterograde axonal transport, was identified as a novel DISC1-interacting molecule. DISC1 directly interacted with kinesin heavy chain of Kinesin-1. Kinesin-1 interacted with the NUDEL/LIS1/14-3-3 complex through DISC1, and these molecules localized mainly at cell bodies and partially in the distal part of the axons. DISC1 partially colocalized with Kinesin family member 5A, NUDEL, LIS1, and 14-3-3 in the growth cones. The knockdown of DISC1 by RNA interference or the dominant-negative form of DISC1 inhibited the accumulation of NUDEL, LIS1, and 14-3-3 at the axons and axon elongation. The knockdown or the dominant-negative form of Kinesin-1 inhibited the accumulation of DISC1 at the axons and axon elongation. Furthermore, the knockdown of NUDEL or LIS1 inhibited axon elongation. Together, these results indicate that DISC1 regulates the localization of NUDEL/LIS1/14-3-3 complex into the axons as a cargo receptor for axon elongation.

Key words: DISC1; Kinesin-1; axonal transport; axon elongation; schizophrenia; NUDEL

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Received Sept. 2, 2006; revised Oct. 31, 2006; accepted Nov. 24, 2006.

Correspondence should be addressed to Dr. Kozo Kaibuchi, Department of Cell Pharmacology, Graduate School of Medicine, Nagoya University, 65 Tsurumai, Showa, Nagoya 466-8550, Japan. Email: kaibuchi{at}med.nagoya-u.ac.jp

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