Yuzuru Imai
  • Department of Research for Parkinson's Disease, Juntendo University Graduate School of Medicine, Japan, Japan,
Research focus
  • Neuroscience
Personal information


Ph.D, Department of Biophysics, Graduate School of Science, Kyoto University, Japan, 1999

Current position

Associate Professor, Department of Research for Parkinson's Disease, Juntendo University, Japan, 2013-2017


  1. Hosaka, Y., Inoshita, T., Shiba-Fukushima, K., Cui, C., Arano, T., Imai, Y. and Hattori, N. (2017). Reduced TDP-43 Expression Improves Neuronal Activities in a Drosophila Model of Perry Syndrome. EBioMedicine 21: 218-227.
  2. Meng, H., Yamashita, C., Shiba-Fukushima, K., Inoshita, T., Funayama, M., Sato, S., Hatta, T., Natsume, T., Umitsu, M., Takagi, J., Imai, Y. and Hattori, N. (2017). Loss of Parkinson's disease-associated protein CHCHD2 affects mitochondrial crista structure and destabilizes cytochrome c. Nat Commun 8: 15500.
  3. Shiba-Fukushima, K., Ishikawa, K. I., Inoshita, T., Izawa, N., Takanashi, M., Sato, S., Onodera, O., Akamatsu, W., Okano, H., Imai, Y. and Hattori, N. (2017). Evidence that phosphorylated ubiquitin signaling is involved in the etiology of Parkinson's disease. Hum Mol Genet 26(16): 3172-3185.
  4. Inoshita, T., Arano, T., Hosaka, Y., Meng, H., Umezaki, Y., Kosugi, S., Morimoto, T., Koike, M., Chang, H. Y., Imai, Y. and Hattori, N. (2017). Vps35 in cooperation with LRRK2 regulates synaptic vesicle endocytosis through the endosomal pathway in Drosophila. Hum Mol Genet 26(15): 2933-2948.
  5. Iyer, J., Wang, Q., Le, T., Pizzo, L., Gronke, S., Ambegaokar, S. S., Imai, Y., Srivastava, A., Troisi, B. L., Mardon, G., Artero, R., Jackson, G. R., Isaacs, A. M., Partridge, L., Lu, B., Kumar, J. P. and Girirajan, S. (2016). Quantitative Assessment of Eye Phenotypes for Functional Genetic Studies Using Drosophila melanogaster. G3 (Bethesda) 6(5): 1427-1437.
  6. Klionsky, D. J., et al. (2016). Guidelines for the use and interpretation of assays for monitoring autophagy (3rd edition). Autophagy 2(1): 1-222.
  7. Imai, Y., Kobayashi, Y., Inoshita, T., Meng, H., Arano, T., Uemura, K., Asano, T., Yoshimi, K., Zhang, C. L., Matsumoto, G., Ohtsuka, T., Kageyama, R., Kiyonari, H., Shioi, G., Nukina, N., Hattori, N. and Takahashi, R. (2015). The Parkinson's Disease-Associated Protein Kinase LRRK2 Modulates Notch Signaling through the Endosomal Pathway. PLoS Genet 11(9): e1005503.
  8. Vaikath, N. N., Majbour, N. K., Paleologou, K. E., Ardah, M. T., van Dam, E., van de Berg, W. D., Forrest, S. L., Parkkinen, L., Gai, W. P., Hattori, N., Takanashi, M., Lee, S. J., Mann, D. M., Imai, Y., Halliday, G. M., Li, J. Y. and El-Agnaf, O. M. (2015). Generation and characterization of novel conformation-specific monoclonal antibodies for alpha-synuclein pathology. Neurobiol Dis 79: 81-99.
  9. Shiba-Fukushima, K., Arano, T., Matsumoto, G., Inoshita, T., Yoshida, S., Ishihama, Y., Ryu, K. Y., Nukina, N., Hattori, N. and Imai, Y. (2014). Phosphorylation of mitochondrial polyubiquitin by PINK1 promotes Parkin mitochondrial tethering. PLoS Genet 10(12): e1004861.
  10. Riley, B. E. and Olzmann, J. A. (2015). A polyubiquitin chain reaction: parkin recruitment to damaged mitochondria. PLoS Genet 11(1): e1004952.
  11. Shiba-Fukushima, K., Inoshita, T., Hattori, N. and Imai, Y. (2014). Lysine 63-linked polyubiquitination is dispensable for Parkin-mediated mitophagy. J Biol Chem 289(48): 33131-33136.
  12. Shiba-Fukushima, K., Inoshita, T., Hattori, N. and Imai, Y. (2014). PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila. PLoS Genet 10(6): e1004391.
  13. Wu, Z., Sawada, T., Shiba, K., Liu, S., Kanao, T., Takahashi, R., Hattori, N., Imai, Y. and Lu, B. (2013). Tricornered/NDR kinase signaling mediates PINK1-directed mitochondrial quality control and tissue maintenance. Genes Dev 27(2): 157-162.
  14. Shiba-Fukushima, K., Imai, Y., Yoshida, S., Ishihama, Y., Kanao, T., Sato, S. and Hattori, N. (2012). PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy. Sci Rep 2: 1002.
  15. Liu, S., Sawada, T., Lee, S., Yu, W., Silverio, G., Alapatt, P., Millan, I., Shen, A., Saxton, W., Kanao, T., Takahashi, R., Hattori, N., Imai, Y. and Lu, B. (2012). Parkinson's disease-associated kinase PINK1 regulates Miro protein level and axonal transport of mitochondria. PLoS Genet 8(3): e1002537.
  16. Kanao, T., Sawada, T., Davies, S. A., Ichinose, H., Hasegawa, K., Takahashi, R., Hattori, N. and Imai, Y. (2012). The nitric oxide-cyclic GMP pathway regulates FoxO and alters dopaminergic neuron survival in Drosophila. PLoS One 7(2): e30958.
  17. Imai, Y. and Lu, B. (2011). Mitochondrial dynamics and mitophagy in Parkinson's disease: disordered cellular power plant becomes a big deal in a major movement disorder. Curr Opin Neurobiol 21(6): 935-941.
  18. Imai, Y., Kanao, T., Sawada, T., Kobayashi, Y., Moriwaki, Y., Ishida, Y., Takeda, K., Ichijo, H., Lu, B. and Takahashi, R. (2010). The loss of PGAM5 suppresses the mitochondrial degeneration caused by inactivation of PINK1 in Drosophila. PLoS Genet 6(12): e1001229.
  19. Kanao, T., Venderova, K., Park, D. S., Unterman, T., Lu, B. and Imai, Y. (2010). Activation of FoxO by LRRK2 induces expression of proapoptotic proteins and alters survival of postmitotic dopaminergic neuron in Drosophila. Hum Mol Genet 19(19): 3747-3758.
  20. Gehrke, S., Imai, Y., Sokol, N. and Lu, B. (2010). Pathogenic LRRK2 negatively regulates microRNA-mediated translational repression. Nature 466(7306): 637-641.
  21. Imai, Y., Gehrke, S., Wang, H. Q., Takahashi, R., Hasegawa, K., Oota, E. and Lu, B. (2008). Phosphorylation of 4E-BP by LRRK2 affects the maintenance of dopaminergic neurons in Drosophila. EMBO J 27(18): 2432-2443.
  22. Wang, H. Q., Imai, Y., Inoue, H., Kataoka, A., Iita, S., Nukina, N. and Takahashi, R. (2008). Pael-R transgenic mice crossed with parkin deficient mice displayed progressive and selective catecholaminergic neuronal loss. J Neurochem 107(1): 171-185.
  23. Wang, J. W., Imai, Y. and Lu, B. (2007). Activation of PAR-1 kinase and stimulation of tau phosphorylation by diverse signals require the tumor suppressor protein LKB1. J Neurosci 27(3): 574-581.
  24. Kitao, Y., Imai, Y., Ozawa, K., Kataoka, A., Ikeda, T., Soda, M., Nakimawa, K., Kiyama, H., Stern, D. M., Hori, O., Wakamatsu, K., Ito, S., Itohara, S., Takahashi, R. and Ogawa, S. (2007). Pael receptor induces death of dopaminergic neurons in the substantia nigra via endoplasmic reticulum stress and dopamine toxicity, which is enhanced under condition of parkin inactivation. Hum Mol Genet 16(1): 50-60.
  25. Yang, Y., Gehrke, S., Imai, Y., Huang, Z., Ouyang, Y., Wang, J. W., Yang, L., Beal, M. F., Vogel, H. and Lu, B. (2006). Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin. Proc Natl Acad Sci U S A 103(28): 10793-10798.
  26. Yang, Y., Gehrke, S., Haque, M. E., Imai, Y., Kosek, J., Yang, L., Beal, M. F., Nishimura, I., Wakamatsu, K., Ito, S., Takahashi, R. and Lu, B. (2005). Inactivation of Drosophila DJ-1 leads to impairments of oxidative stress response and phosphatidylinositol 3-kinase/Akt signaling. Proc Natl Acad Sci U S A 102(38): 13670-13675.
  27. Imai, Y. and Takahashi, R. (2004). How do Parkin mutations result in neurodegeneration? Curr Opin Neurobiol 14(3): 384-389.
  28. Yang, Y., Nishimura, I., Imai, Y., Takahashi, R. and Lu, B. (2003). Parkin suppresses dopaminergic neuron-selective neurotoxicity induced by Pael-R in Drosophila. Neuron 37(6): 911-924.
  29. Imai, Y., Soda, M., Hatakeyama, S., Akagi, T., Hashikawa, T., Nakayama, K. I. and Takahashi, R. (2002). CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity. Mol Cell 10(1): 55-67.
  30. Suzuki, Y., Imai, Y., Nakayama, H., Takahashi, K., Takio, K. and Takahashi, R. (2001). A serine protease, HtrA2, is released from the mitochondria and interacts with XIAP, inducing cell death. Mol Cell 8(3): 613-621.
  31. Imai, Y., Soda, M., Inoue, H., Hattori, N., Mizuno, Y. and Takahashi, R. (2001). An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 105(7): 891-902.
  32. Imai, Y., Soda, M. and Takahashi, R. (2000). Parkin suppresses unfolded protein stress-induced cell death through its E3 ubiquitin-protein ligase activity. J Biol Chem 275(46): 35661-35664.
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