Asada, N. and Sanada, K. (2010). LKB1-Mediated Spatial Control of GSK3 and
Adenomatous Polyposis Coli Contributes to Centrosomal Forward Movement and
Neuronal Migration in the Developing Neocortex. J. Neurosci. 30, 8852–8865.
Asada, N., Sanada, K. and Fukada, Y. (2007). LKB1 Regulates Neuronal Migration
and Neuronal Differentiation in the Developing Neocortex through Centrosomal
Positioning. J. Neurosci. 27, 11769–11775.
Bellion, A., Baudoin, J. P., Alvarez, C., Bornens, M. and Métin, C. (2005).
Nucleokinesis in tangentially migrating neurons comprises two alternating phases:
Forward migration of the Golgi/centrosome associated with centrosome splitting
and myosin contraction at the rear. J. Neurosci. 25, 5691–5699.
Bertipaglia, C., Gonçalves, J. C. and Vallee, R. B. (2018). Nuclear migration in
mammalian brain development. Semin. Cell Dev. Biol. 82, 57–66.
Blasier, K. R., Humsi, M. K., Ha, J., Ross, M. W., Smiley, W. R., Inamdar, N. A.,
Mitchell, D. J., Lo, K. W. H. and Pfister, K. K. (2014). Live cell imaging reveals
differential modifications to cytoplasmic dynein properties by phospho- and
dephosphomimic mutations of the intermediate chain 2C S84. J. Neurosci. Res. 92,
1143–1154.
Burkhardt, J. K., Echeverri, C. J., Nilsson, T. and Vallee, R. B. (1997).
Overexpression of the dynamitin (p50) subunit of the dynactin complex disrupts
dynein-dependent maintenance of membrane organelle distribution. J. Cell Biol.
139, 469–484.
Cooper, J. A. (2013). Mechanisms of cell migration in the nervous system. J. Cell Biol.
202, 725–734.
56
Dasgupta, B. and Chhipa, R. R. (2016). Evolving Lessons on the Complex Role of
AMPK in Normal Physiology and Cancer. Trends Pharmacol. Sci. 37, 192–206.
Echeverri, C. J., Paschal, B. M., Vaughan, K. T. and Vallee, R. B. (1996). Molecular
characterization of the 50-kD subunit of dynactin reveals function for the complex
in chromosome alignment and spindle organization during mitosis. J. Cell Biol.
132, 617–633.
Feng, Y. and Walsh, C. A. (2001). Protein–Protein interactions, cytoskeletal regulation
and neuronal migration . Nat. Rev. Neurosci. 2, 408–416.
Gao, F. J., Hebbar, S., Gao, X. A., Alexander, M., Pandey, J. P., Walla, M. D.,
Cotham, W. E., King, S. J. and Smith, D. S. (2015). GSK-3β Phosphorylation of
Cytoplasmic Dynein Reduces Ndel1 Binding to Intermediate Chains and Alters
Dynein Motility. Traffic 16, 941–961.
Ginty, D. D. and Segal, R. A. (2002). Retrograde neurotrophin signaling: Trk-ing
along the axon. Curr. Opin. Neurobiol. 12, 268–274.
Guerrini, R. and Parrini, E. (2010). Neuronal migration disorders. Neurobiol. Dis. 38,
154–166.
Harada, A., Takei, Y., Kanai, Y., Tanaka, Y., Nonaka, S. and Hirokawa, N. (1998).
Golgi vesiculation and lysosome dispersion in cells lacking cytoplasmic dynein. J.
Cell Biol. 141, 51–59.
Hatten, M. E. (1999). CENTRAL NERVOUS SYSTEM NEURONAL MIGRATION.
Annu. Rev. Neurosci. 22, 511–539.
Jaleel, M., McBride, A., Lizcano, J. M., Deak, M., Toth, R., Morrice, N. A. and
Alessi, D. R. (2005). Identification of the sucrose non-fermenting related kinase
SNRK, as a novel LKB1 substrate. FEBS Lett. 579, 1417–1423.
57
Jeon, S.-M. (2016). Regulation and function of AMPK in physiology and diseases. Exp.
Mol. Med. 48, e245–e245.
Kato, M. and Dobyns, W. B. (2003). Lissencephaly and the molecular basis of
neuronal migration. Hum. Mol. Genet. 12, R89–R96.
Kinoshita, E., Kinoshita-Kikuta, E., Takiyama, K. and Koike, T. (2005). Phosphatebinding Tag, a New Tool to Visualize Phosphorylated Proteins. Mol. Cell.
Proteomics 5, 749–757.
Kriegstein, A. R. and Noctor, S. C. (2004). Patterns of neuronal migration in the
embryonic cortex. Trends Neurosci. 27, 392–399.
Kuta, A., Deng, W., Morsi El-Kadi, A., Banks, G. T., Hafezparast, M., Pfister, K.
K. and Fisher, E. M. C. (2010). Mouse Cytoplasmic Dynein Intermediate Chains:
Identification of New Isoforms, Alternative Splicing and Tissue Distribution of
Transcripts. PLoS One 5, e11682.
Lizcano, J. M., Göransson, O., Toth, R., Deak, M., Morrice, N. A., Boudeau, J.,
Hawley, S. A., Udd, L., Mäkelä, T. P., Hardie, D. G., et al. (2004). LKB1 is a
master kinase that activates 13 kinases of the AMPK subfamily, including
MARK/PAR-1. EMBO J. 23, 833–843.
Marín, O., Valiente, M., Ge, X. and Tsai, L. H. (2010). Guiding neuronal cell
migrations. Cold Spring Harb. Perspect. Biol. 2, 1–21.
Mitchell, D. J., Blasier, K. R., Jeffery, E. D., Ross, M. W., Pullikuth, A. K., Suo, D.,
Park, J., Smiley, W. R., Lo, K. W.-H., Shabanowitz, J., et al. (2012). Trk
Activation of the ERK1/2 Kinase Pathway Stimulates Intermediate Chain
Phosphorylation and Recruits Cytoplasmic Dynein to Signaling Endosomes for
Retrograde Axonal Transport. J. Neurosci. 32, 15495–15510.
58
Pfister, K. K., Salata, M. W., Dillman, J. F., Torre, E. and Lye, R. J. (1996a).
Identification and developmental regulation of a neuron-specific subunit of
cytoplasmic dynein. Mol. Biol. Cell 7, 331–43.
Pfister, K. K., Salata, M. W., Dillman, J. F., Vaughan, K. T., Vallee, R. B., Torre,
E. and Lye, R. J. (1996b). Differential expression and phosphorylation of the 74kDa intermediate chains of cytoplasmic dynein in cultured neurons and glia. J.
Biol. Chem. 271, 1687–1694.
Reiner, O., Karzbrun, E., Kshirsagar, A. and Kaibuchi, K. (2016). Regulation of
neuronal migration, an emerging topic in autism spectrum disorders. J.
Neurochem. 136, 440–456.
Roghi, C. and Allan, V. J. (1999). Dynamic association of cytoplasmic dynein heavy
chain 1a with the Golgi apparatus and intermediate compartment. J. Cell Sci. 112,
4673 LP – 4685.
Salina, D., Bodoor, K., Eckley, D. M., Schroer, T. A., Rattner, J. B. and Burke, B.
(2002). Cytoplasmic dynein as a facilitator of nuclear envelope breakdown. Cell
108, 97–107.
Schaar, B. T. and McConnell, S. K. (2005). Cytoskeletal coordination during neuronal
migration. Proc. Natl. Acad. Sci. U. S. A. 102, 13652–13657.
Schroer, T. A. (2004). DYNACTIN. Annu. Rev. Cell Dev. Biol. 20, 759–779.
Shu, T., Ayala, R., Nguyen, M. D., Xie, Z., Gleeson, J. G. and Tsai, L. H. (2004).
Ndel1 operates in a common pathway with LIS1 and cytoplasmic dynein to
regulate cortical neuronal positioning. Neuron 44, 263–277.
Solecki, D. J., Trivedi, N., Govek, E. E., Kerekes, R. A., Gleason, S. S. and Hatten,
M. E. (2009). Myosin II motors and F-actin dynamics drive the coordinated
59
movement of the centrosome and soma during CNS glial-guided neuronal
migration. Neuron 63, 63–80.
Stein, S. C., Woods, A., Jones, N. A., Davison, M. D. and Carling, D. (2000). The
regulation of AMP-activated protein kinase by phosphorylation. Biochem. J. 345
Pt 3, 437–443.
Tanaka, T., Serneo, F. F., Higgins, C., Gambello, M. J., Wynshaw-Boris, A. and
Gleeson, J. G. (2004). Lis1 and doublecortin function with dynein to mediate
coupling of the nucleus to the centrosome in neuronal migration. J. Cell Biol. 165,
709–721.
Tsai, L. H. and Gleeson, J. G. (2005). Nucleokinesis in neuronal migration. Neuron
46, 383–388.
Tsai, J. W., Bremner, K. H. and Vallee, R. B. (2007). Dual subcellular roles for LIS1
and dynein in radial neuronal migration in live brain tissue. Nat. Neurosci. 10,
970–979.
Tuerk, R. D., Thali, R. F., Auchli, Y., Rechsteiner, H., Brunisholz, R. A.,
Schlattner, U., Wallimann, T. and Neumann, D. (2007). New Candidate Targets
of AMP-Activated Protein Kinase in Murine Brain Revealed by a Novel
Multidimensional Substrate-Screen for Protein Kinases. J. Proteome Res. 6, 3266–
3277.
Whyte, J., Bader, J. R., Tauhata, S. B. F., Raycroft, M., Hornick, J., Pfister, K. K.,
Lane, W. S., Chan, G. K., Hinchcliffe, E. H., Vaughan, P. S., et al. (2008).
Phosphorylation regulates targeting of cytoplasmic dynein to kinetochores during
mitosis. J. Cell Biol. 183, 819–834.
Williams, T., Courchet, J., Viollet, B., Brenman, J. E. and Polleux, F. (2011). AMP60
activated protein kinase (AMPK) activity is not required for neuronal development
but regulates axogenesis during metabolic stress. Proc. Natl. Acad. Sci. 108, 5849–
5854.
Zhang, X., Lei, K., Yuan, X., Wu, X., Zhuang, Y., Xu, T., Xu, R. and Han, M.
(2009). SUN1/2 and Syne/Nesprin-1/2 Complexes Connect Centrosome to the
Nucleus during Neurogenesis and Neuronal Migration in Mice. Neuron 64, 173–
187.
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7. Acknowledgements
I would like to show my greatest appreciation to my supervisor, Professor Yoshikado
Sanada, for his valuable discussion and advice. I would like to appreciate Dr. Naoyuki
Asada for his helpful comments and advice for experimental techniques. I am grateful to
Dr. Minh Dang Nguyen for his advice, to Dr. Takahiko Matsuda for providing
pCAGEN, pCAGIG, pCAG-CFP plasmids, to Dr. Li-Huei Tsai for providing the Dynein
HC shRNA plasmid, to Dr. Yang Shi for providing the pBS-U6 plasmid. I would like to
thank Dr. Nobuhiro Kurabayashi and the other members of Sanada laboratory for their
valuable suggestions and discussion.
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