Kazuhisa Nakayama Department of Physiological Chemistry, Graduate School and Faculty of Pharmaceutical Sciences, Kyoto University, Japan, Japan,
1 protocol

Kentaro Nakamura Department of Physiological Chemistry, Graduate School and Faculty of Pharmaceutical Sciences, Kyoto University, Japan, Japan,
1 protocol

Yohei Katoh
  • Department of Physiological Chemistry, Graduate School and Faculty of Pharmaceutical Sciences, Kyoto University, Japan, Japan,
Research focus
  • Neuroscience
  • 1 Author merit


Ph.D., Graduate School of Pharmaceutical Sciences, Kyoto University, Japan, 2007

Current position

Assistant Professor, Department of Physiological Chemistry, Graduate School of Pharmaceutical Sciences, Kyoto University, Japan


  1. Nakayama, K. and Katoh, Y. (2017). Ciliary protein trafficking mediated by IFT and BBSome complexes with the aid of kinesin-2 and dynein-2 motors. J Biochem.
  2. Takahara, M., Katoh, Y., Nakamura, K., Hirano, T., Sugawa, M., Tsurumi, Y. and Nakayama, K. (2017). Ciliopathy-associated mutations of IFT122 impair ciliary protein trafficking but not ciliogenesis. Hum Mol Genet.
  3. Nishijima, Y., Hagiya, Y., Kubo, T., Takei, R., Katoh, Y. and Nakayama, K. (2017). RABL2 interacts with the intraflagellar transport-B complex and CEP19 and participates in ciliary assembly. Mol Biol Cell 28(12): 1652-1666.
  4. Katoh, Y., Michisaka, S., Nozaki, S., Funabashi, T., Hirano, T., Takei, R. and Nakayama, K. (2017). Practical method for targeted disruption of cilia-related genes by using CRISPR/Cas9-mediated, homology-independent knock-in system. Mol Biol Cell 28(7): 898-906.
  5. Funabashi, T., Katoh, Y., Michisaka, S., Terada, M., Sugawa, M. and Nakayama, K. (2017). Ciliary entry of KIF17 is dependent on its binding to the IFT-B complex via IFT46-IFT56 as well as on its nuclear localization signal. Mol Biol Cell 28(5): 624-633.
  6. Hirano, T., Katoh, Y. and Nakayama, K. (2017). Intraflagellar transport-A complex mediates ciliary entry and retrograde trafficking of ciliary G protein-coupled receptors. Mol Biol Cell 28(3): 429-439.
  7. Nozaki, S., Katoh, Y., Terada, M., Michisaka, S., Funabashi, T., Takahashi, S., Kontani, K. and Nakayama, K. (2017). Regulation of ciliary retrograde protein trafficking by the Joubert syndrome proteins ARL13B and INPP5E. J Cell Sci 130(3): 563-576.
  8. Tanaka, Y., Ono, N., Shima, T., Tanaka, G., Katoh, Y., Nakayama, K., Takatsu, H. and Shin, H. W. (2016). The phospholipid flippase ATP9A is required for the recycling pathway from the endosomes to the plasma membrane. Mol Biol Cell 27(24): 3883-3893.
  9. Katoh, Y., Terada, M., Nishijima, Y., Takei, R., Nozaki, S., Hamada, H. and Nakayama, K. (2016). Overall Architecture of the Intraflagellar Transport (IFT)-B Complex Containing Cluap1/IFT38 as an Essential Component of the IFT-B Peripheral Subcomplex. J Biol Chem 291(21): 10962-10975.
  10. Hamamoto, A., Yamato, S., Katoh, Y., Nakayama, K., Yoshimura, K., Takeda, S., Kobayashi, Y. and Saito, Y. (2016). Modulation of primary cilia length by melanin-concentrating hormone receptor 1. Cell Signal 28(6): 572-584.
  11. Katoh, Y., Nozaki, S., Hartanto, D., Miyano, R. and Nakayama, K. (2015). Architectures of multisubunit complexes revealed by a visible immunoprecipitation assay using fluorescent fusion proteins. J Cell Sci 128(12): 2351-2362.
  12. Kubo, K., Kobayashi, M., Nozaki, S., Yagi, C., Hatsuzawa, K., Katoh, Y., Shin, H. W., Takahashi, S. and Nakayama, K. (2015). SNAP23/25 and VAMP2 mediate exocytic event of transferrin receptor-containing recycling vesicles. Biol Open 4(7): 910-920.
  13. Takatsu, H., Katoh, Y., Ueda, T., Waguri, S., Murayama, T., Takahashi, S., Shin, H. W. and Nakayama, K. (2013). Mitosis-coupled, microtubule-dependent clustering of endosomal vesicles around centrosomes. Cell Struct Funct 38(1): 31-41.
  14. Kondo, Y., Hanai, A., Nakai, W., Katoh, Y., Nakayama, K. and Shin, H. W. (2012). ARF1 and ARF3 are required for the integrity of recycling endosomes and the recycling pathway. Cell Struct Funct 37(2): 141-154.
  15. Takahashi, S., Kubo, K., Waguri, S., Yabashi, A., Shin, H. W., Katoh, Y. and Nakayama, K. (2012). Rab11 regulates exocytosis of recycling vesicles at the plasma membrane. J Cell Sci 125(Pt 17): 4049-4057.
  16. Makyio, H., Ohgi, M., Takei, T., Takahashi, S., Takatsu, H., Katoh, Y., Hanai, A., Ueda, T., Kanaho, Y., Xie, Y., Shin, H. W., Kamikubo, H., Kataoka, M., Kawasaki, M., Kato, R., Wakatsuki, S. and Nakayama, K. (2012). Structural basis for Arf6-MKLP1 complex formation on the Flemming body responsible for cytokinesis. EMBO J 31(11): 2590-2603.
  17. Yamamoto, H., Koga, H., Katoh, Y., Takahashi, S., Nakayama, K. and Shin, H. W. (2010). Functional cross-talk between Rab14 and Rab4 through a dual effector, RUFY1/Rabip4. Mol Biol Cell 21(15): 2746-2755.
  18. Katoh, Y., Ritter, B., Gaffry, T., Blondeau, F., Honing, S. and McPherson, P. S. (2009). The clavesin family, neuron-specific lipid- and clathrin-binding Sec14 proteins regulating lysosomal morphology. J Biol Chem 284(40): 27646-27654.
  19. Yanagida-Ishizaki, Y., Takei, T., Ishizaki, R., Imakagura, H., Takahashi, S., Shin, H. W., Katoh, Y. and Nakayama, K. (2008). Recruitment of Tom1L1/Srcasm to endosomes and the midbody by Tsg101. Cell Struct Funct 33(1): 91-100.
  20. Katoh, Y., Imakagura, H., Futatsumori, M. and Nakayama, K. (2006). Recruitment of clathrin onto endosomes by the Tom1-Tollip complex. Biochem Biophys Res Commun 341(1): 143-149.
  21. Akutsu, M., Kawasaki, M., Katoh, Y., Shiba, T., Yamaguchi, Y., Kato, R., Kato, K., Nakayama, K. and Wakatsuki, S. (2005). Structural basis for recognition of ubiquitinated cargo by Tom1-GAT domain. FEBS Lett 579(24): 5385-5391.
  22. Katoh, Y., Shiba, Y., Mitsuhashi, H., Yanagida, Y., Takatsu, H. and Nakayama, K. (2004). Tollip and Tom1 form a complex and recruit ubiquitin-conjugated proteins onto early endosomes. J Biol Chem 279(23): 24435-24443.
  23. Shiba, Y., Katoh, Y., Shiba, T., Yoshino, K., Takatsu, H., Kobayashi, H., Shin, H. W., Wakatsuki, S. and Nakayama, K. (2004). GAT (GGA and Tom1) domain responsible for ubiquitin binding and ubiquitination. J Biol Chem 279(8): 7105-7111.
  24. Takatsu, H., Katoh, Y., Shiba, Y. and Nakayama, K. (2001). Golgi-localizing, gamma-adaptin ear homology domain, ADP-ribosylation factor-binding (GGA) proteins interact with acidic dileucine sequences within the cytoplasmic domains of sorting receptors through their Vps27p/Hrs/STAM (VHS) domains. J Biol Chem 276(30): 28541-28545.
1 Protocol published
Visible Immunoprecipitation (VIP) Assay: a Simple and Versatile Method for Visual Detection of Protein-protein Interactions
Authors:  Yohei Katoh, Kentaro Nakamura and Kazuhisa Nakayama, date: 01/05/2018, view: 8292, Q&A: 0
The visible immunoprecipitation (VIP) assay is a convenient alternative to conventional co-immunoprecipitation (Katoh et al., 2015). By processing lysates from cells co-expressing GFP-fusion and RFP-fusion proteins for immunoprecipitation ...
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