Integrative Life Sciences :
Cellular Network


Professor FUKUDA Mitsunori
Campus Aobayama campus
Laboratory Membrane Trafficking Mechanisms
Tel +81-22-795-7731
E-mail nori@tohoku.ac.jp
Website http://www.biology.tohoku.ac.jp/lab-www/fukuda_lab/home-ja.html http://www.ac.cyberhome.ne.jp/~fukuda/top_page.htm


Google Scholar


My hobbies are nature watching and sports, but professionally I am advancing research involving membrane trafficking. I am searching for ambitious students looking to be future researchers.

Don’t hesitate to get in touch with me!

1990 Graduated, Biological Institute, Faculty of Science, Tohoku University
1992 Completed master’s program, Department of Biology, Graduate School of Science, Tohoku University
1996 Completed doctoral program, Graduate School of Medicine, The University of Tokyo
  Research Fellowship for Young Scientists, JSPS
1998 Research Scientist, Laboratory for Developmental Neurobiology, RIKEN Brain Science Institute
2002 Unit Leader, Fukuda Initiative Research Unit, RIKEN
2006 Professor, Graduate School of Life Sciences, Tohoku University
Selected Publications
  1. Nakashima, S., Matsui, T. and Fukuda, M. (2023) Vps9d1 regulates tubular endosome formation through specific activation of Rab22A. J. Cell Sci. 136, jcs260522
  2. Hiragi, S., Matsui, T., Sakamaki, Y. and Fukuda, M. (2022) TBC1D18 is a Rab5-GAP that coordinates endosome maturation together with Mon1. J. Cell Biol. 221, e202201114
  3. Matsui, T., Sakamaki, Y., Nakashima, S. and Fukuda, M. (2022) Rab39 and its effector UACA regulate basolateral exosome release from polarized epithelial cells. Cell Rep. 39, 110875
  4. Maruta, Y. and Fukuda, M. (2022) Large Rab GTPase Rab44 regulates microtubule-dependent retrograde melanosome transport in melanocytes. J. Biol. Chem. 298, 102508
  5. Hatoyama, Y., Homma, Y., Hiragi, S. and Fukuda, M. (2021) Establishment and analysis of conditional Rab1- and Rab5-knockout cells using the auxin-inducible degron system. J. Cell Sci. 134, jcs259184
  6. Matsui, T., Osaki, F., Hiragi, S., Sakamaki, Y. and Fukuda, M. (2021) ALIX and ceramide differentially control polarized small extracellular vesicle release from epithelial cells. EMBO Rep. 22, e51475
  7. Osaki, F., Matsui, T., Hiragi, S., Homma, Y. and Fukuda, M. (2021) RBD11, a bioengineered Rab11-binding module for visualizing and analyzing endogenous Rab11. J. Cell Sci. 134, jcs257311
  8. Oguchi, M. E., Okuyama, K., Homma, Y. and Fukuda, M. (2020) A comprehensive analysis of Rab GTPases reveals a role for Rab34 in serum starvation-induced primary ciliogenesis. J. Biol. Chem. 295, 12674-12685
  9. Homma, Y., Kinoshita, R., Kuchitsu, Y., Wawro, P. S., Marubashi, S., Oguchi, M. E., Ishida, M., Fujita, N. and Fukuda, M. (2019) Comprehensive knockout analysis of the Rab family GTPases in epithelial cells. J. Cell Biol. 218, 2035-2050
  10. Etoh, K. and Fukuda, M. (2019) Rab10 regulates tubular endosome formation through KIF13A and KIF13B motors. J. Cell Sci. 132, jcs226977
  11. Kuchitsu, Y., Homma, Y., Fujita, N. and Fukuda, M. (2018) Rab7 knockout unveils regulated autolysosome maturation induced by glutamine starvation. J. Cell Sci. 131, jcs215442
  12. Fujita, N., Huang, W., Lin, T.-H., Groulx, J.-F., Jean, S., Nguyen, J., Kuchitsu, Y., Koyama-Honda, I., Mizushima, N., Fukuda, M. and Kiger, A. A. (2017) Genetic screen in Drosophila muscle identifies autophagy-mediated T-tubule remodeling and a Rab2 role in autophagy. eLife 6, e23367
  13. Homma, Y. and Fukuda, M. (2016) Rabin8 regulates neurite outgrowth in both GEF-activity-dependent and -independent manners. Mol. Biol. Cell 27, 2107-2118
  14. Mrozowska, P. S. and Fukuda, M. (2016) Regulation of podocalyxin trafficking by Rab small GTPases in 2D and 3D epithelial cell cultures. J. Cell Biol. 213, 355-369
  15. Marubashi, S., Shimada, H., Fukuda, M. & Ohbayashi, N. (2016) RUTBC1 functions as a GTPase-activating protein for Rab32/38 and regulates melanogenic enzyme trafficking in melanocytes. J. Biol. Chem. 291, 1427-1440
  16. Hirano, S., Uemura, T., Annoh, H., Fujita, N., Waguri, S., Itoh, T. & Fukuda, M. (2016) Differing susceptibility to autophagic degradation activity of two LC3-binding proteins: SQSTM1/p62 and TBC1D25/OATL1. Autophagy 12, 312-326
  17. Aizawa, M. & Fukuda, M. (2015) Small GTPase Rab2B and its specific binding protein Golgi-associated Rab2B interactor-like 4 (GARI-L4) regulate Golgi morphology. J. Biol. Chem. 290, 22250-22261
  18. Etoh, K. &  Fukuda, M. (2015) Structure-function analyses of the small GTPase Rab35 and its efffector protein centaurin-β2/ACAP2 during neurite outgrowth of PC12 cells. J. Biol. Chem. 290, 9064-9074
  19. Yatsu, A., Shimada, H., Ohbayashi, N. & Fukuda, M. (2015) Rab40C is a novel Varp-binding protein that promotes proteasomal degradation of Varp in melanocytes. Biol. Open  4, 267-275
  20. Ishida, M., Ohbayashi, N. & Fukuda, M. (2015) Rab1A regulates anterograde melanosome transport by recruiting kinesin-1 to melanosomes through interaction with SKIP. Sci. Rep. 5, 8238
  21. Yasuda, T. & Fukuda, M. (2014) Slp2-a controls renal epithelial cell size through regulation of Rap–ezrin signaling independently of Rab27. J. Cell Sci.127, 557-570
  22. Matsui, T. & Fukuda, M. (2013) Rab12 regulates mTORC1 activity and autophagy through controlling the degradation of amino-acid transporter PAT4. EMBO Rep.
    14, 450-457 
  23. Yatsu, A., Ohbayashi, N., Tamura, K. & Fukuda, M. (2013) Syntaxin-3 is required for melanosomal localization of Tyrp1 in melanocytes. J. Invest. Dermatol. 133, 2237-2246 
  24. Kobayashi, H. & Fukuda, M. (2013) Rab35 establishes the EHD1-association site by coordinating two distinct effectors during neurite outgrowth. J. Cell Sci. 126, 2424-2435
  25. Yasuda, T., Saegusa, C., Kamakura, S., Sumimoto, H. & Fukuda, M. (2012) Rab27 effector Slp2-a transports the apical signaling molecule podocalyxin to the apical surface of MDCK II cells and regulates claudin-2 expression. Mol. Biol. Cell 23, 3229-3239
  26. Ishida, M., Ohbayashi, N., Maruta, Y., Ebata, Y. & Fukuda, M. (2012) Functional involvement of Rab1A in microtubule-dependent anterograde melanosome transport in melanocytes. J. Cell Sci. 125, 5177-5187 
  27. Kobayashi, H. & Fukuda, M. (2012) Rab35 regulates Arf6 activity through centaurin-β2 (ACAP2) during neurite outgrowth. J. Cell Sci. 125, 2235-2243
  28. Ohbayashi, N., Maruta, Y., Ishida, M. & Fukuda, M. (2012) Melanoregulin regulates retrograde melanosome transport through interaction with the RILP-p150Glued complex in melanocytes. J. Cell Sci. 125, 1508-1518
  29. Mori, Y., Matsui, T., Furutani, Y., Yoshihara, Y. & Fukuda, M. (2012) Small GTPase Rab17 regulates dendritic morphogenesis and postsynaptic development of ippocampal neurons. J. Biol. Chem. 287, 8963-8973
  30. Matsui, T., Itoh, T. & Fukuda, M. (2011) Small GTPase Rab12 regulates constitutive degradation of transferrin receptor. Traffic 12, 1432-1443 
  31. Itoh, T., Kanno, E., Uemura, T., Waguri, S. & Fukuda, M. (2011) OATL1, a novel autophagosome-resident Rab33B-GAP, regulates autophagosomal maturation. J. Cell Biol. 192, 839-853  
  32. Tamura, K., Ohbayashi, N., Ishibashi, K. & Fukuda, M. (2011) Structure-function analysis of VPS9-ankyrin-repeat protein (Varp) in the trafficking of tyrosinase-related protein 1 in melanocytes. J. Biol. Chem. 286, 7507-7521 
  33. Kanno, E., Ishibashi, K., Kobayashi, H., Matsui, T., Ohbayashi, N. & Fukuda, M. (2010) Comprehensive screening for novel Rab-binding proteins by GST pull-down assay using 60 different mammalian Rabs. Traffic 11, 491-507 
  34. Tamura, K., Ohbayashi, N., Maruta, Y., Kanno, E., Itoh, T. & Fukuda, M. (2009) Varp is a novel Rab32/38-binding protein that regulates Tyrp1 trafficking in melanocytes. Mol. Biol. Cell 20, 2900-2908 
  35. Fukuda, M., Kanno, E., Ishibashi, K. & Itoh, T. (2008) Large scale screening for novel Rab effectors reveals unexpected broad Rab binding specificity. Mol. Cell. Proteomics 7, 1031-1042 
  36. Itoh, T., Fujita, N., Kanno, E., Yamamoto, A., Yoshimori, T. & Fukuda, M. (2008) Golgi-resident small GTPase Rab33B interacts with Atg16L and modulates autophagosome formation. Mol. Biol. Cell 19, 2916-2925 
  37. Yu, E., Kanno, E., Choi, S., Sugimori, M., Moreira, J. E., Llinas, R. R. & Fukuda, M. (2008) Role of Rab27 in synaptic transmission at the squid giant synapse. Proc. Natl. Acad. Sci. USA 105, 16003-16008

Please see http://www.ac.cyberhome.ne.jp/~fukuda/top_page.htm for other publications.

Activities in Academic Societies

Japanese Biochemical Society, Molecular Biology Society of Japan, Japan Society for Cell Biology, Japan Neuroscience Society, Japanese Society for Pigment Cell Research, American Society for Biochemistry and Molecular Biology, American Society for Cell Biology


Life Science A-C (General Education),
Molecular cell biology I (Undergraduate),
Advanced Cell Biology I-IV (Graduate School), etc.

Recent Activities

Our bodies are made up of several tens of trillions of cells, which individually are considered to be the fundamental units of life. Various small organs, covered in membranes and called organelles, exist inside cells. Although these organelles possess unique functions, they do not exist independently of each other, but rather frequently exchange information by transport of membrane-wrapped substances (generally called membrane trafficking). Because defects in appropriate membrane trafficking causes a variety of human diseases, understanding the molecular mechanisms behind membrane trafficking is an important research challenge in biology and medical science. The existence of “traffic controllers” is important for the regulation of membrane trafficking, and in our laboratory we focus on the Rab protein, which acts as a traffic controller, to understand the molecular mechanisms underlying membrane trafficking. Although various kinds of membrane trafficking occur inside cells, in our laboratory we are particularly interested in autophagy, neuron-specific membrane trafficking such as the release of neurotransmitters, in addition to melanosome transport in melanocytes; and we are engaged in revealing the molecular mechanisms behind them.

fukuda image1

Message to Students

Biology remains an academic field, which is not fully established. Although our understanding of the molecular mechanisms behind biological phenomena has grown by leaps and bounds in recent years due to the development of molecular biology, there still remains a mountain of information that we have not yet discovered. In other words, there are enormous opportunities for young people aspiring to engage in life sciences research in the future. Why not explore the mysteries of life together with us?