学术活动
导师介绍

Yoji Kawano
青年研究组长,博士生导师


Email: yoji.kawano@sibs.ac.cn
Phone:(86) 21- 57078279

个人简介:
2015.1- 至今 中科院上海植物逆境生物学研究中心,青年研究组长、硕士生导师

2006.1-2014.12 日本 奈良先端科学技術大学院大学,助理教授、博士后

2005.4-2005.9 日本独协医科大学,助理教授

2001.4-2005.3 日本名古屋大学,博士后

1999-2001 日本 奈良先端科学技术大学院大学,生物科学,博士

1997-1999 日本奈良先端科学技术大学院大学,生物科学,硕士

1993-1997 日本鸟取大学农学专业,学士

研究方向:

信号转导和免疫学

研究工作:
A master regulator of immunity, OsRac1, and R protein signaling

Resistance (R) proteins are crucial intracellular receptors that detect attack by insects and invasion by various pathogens including fungi, bacteria and viruses. However, the signaling molecules that mediate R protein-induced immune responses are not yet fully understood. We have previously shown that an intracellular switch, the small GTPase OsRac1, is a master regulator controlling immunity in rice (Kawano et al., 2010b, Kawano and Shimamoto, 2013). However, the mechanism by which OsRac1 receives signals from the immune receptors and becomes activated has remained unclear. Thus, we explored OsRac1-binding proteins and identified the R protein Pit, which is a immune receptor for rice blast fungus, a prominent microbial disease of rice (Kawano et al., 2010a). Through various analyses, we demonstrated that OsRac1 functions as a molecular switch, controlling ROS production and hypersensitive cell death downstream of Pit. In addition, we have found that anchoring Pit to the plasma membrane through palmitoylation, a type of lipid modification is required for Pit-induced activation of OsRac1 on the plasma membrane (Kawano et al., 2014). Our work has therefore revealed the signaling pathway of the R protein Pit through OsRac1.


In vivo monitoring of OsRac1 activity and chitin-triggered immunity

Given that the small GTPase OsRac1 is a master regulator controlling rice immunity, monitoring its activation within plant cells was believed to be the next key step in understanding plant immunity. By creating a bio-imaging sensor using the Forester resonance energy transfer (FRET) of fluorescent proteins, we were the first to successfully monitor the activation of a plant small GTPase in vivo (Kawano et al., 2010a). Using this sensor, we identified the R protein Pit as an immune receptor that activated OsRac1 on the plasma membrane (Kawano et al., 2010a), and observed that OsRac1 was activated within 3 min after sensing chitin, a cell wall component of rice blast fungus (Akamatsu et al., 2013). Furthermore, we revealed that the signal from the chitin receptor OsCERK1 was transmitted to OsRac1 through the OsRac1 activator protein OsRacGEF1. We have also reported that OsRac1 controls the expression of defense-related genes through the MAPK OsMPK6 and the transcription factors RAI1 and Rap2.6 (Kim et al., 2012, Wamaitha et al., 2012).



Homologous recombination-based gene targeting of OsRac1 to enhance rice immunity

Over expression of defense-related proteins often causes stress and results in a reduction of biomass. Thus, technological innovation has been considered essential to provide plants with improved resistance to diseases while maintaining biomass. Rice transformed with constitutively active OsRac1 (OsRac1 G19V), which was over expressed using the 35S promoter that allows constant high expression, displays improved resistance against pathogens, but a reduced yield of rice because of a reduction in fertility. Therefore, rather than utilizing conventional gene transfer methods, we applied a gene-targeting method that uses homologous recombination, developed by Dr. R. Terada of Meijo University. Using this method, we introduced a point mutation that makes the endogenous OsRac1 gene constitutively active and investigated whether disease resistance in rice could be improved, thereby avoiding agriculturally unfavorable characters (Dang et al., 2013). Because selection markers can be removed through site-specific recombination, the gene-targeting method utilized in this study is a groundbreaking, marker-free genetic engineering technique with the ability to modify targeted genes as closely as possible to natural mutations. Introduction of the constitutively active mutation into the OsRac1 gene caused an increase in the expression of transcription factors such as WRKY, and of defense-related genes including PAL1 and PBZ1. A resistance response similar to hypersensitive cell death was also observed at the site of rice blast fungus infection.

代表性论文:
2016
Nagano,M., Ishikawa, T., Fujiwara, M., Fukao, Y., Kawano, Y., Kawai-Yamada, M., and Shimamoto, K. (2016) Plasma membrane microdomains are essential for OsRac1-OsRbohB/H-mediated immunity in rice. Plant Cell 28:1966-83

Akamatsu, A., Shimamoto, K., and Kawano, Y. (2016) Crosstalk of Signaling Mechanisms Involved in Host Defense and Symbiosis against Microorganisms in Rice. Curr Genomic 17:1-17

2015
Akamatsu, A., Uno, K., Kato, M., Wong, HL., Shimamoto, K., and Kawano, Y. (2015) New insights into the dimerization of small GTPase Rac/ROP guanine nucleotide exchange factors in rice. Plant Signal Behav. In press

2014
Liu, L., Park, CH., He, F., Nagano, M., Wang, M., Bellizzi, M., Zeng, X., Liu, W., Ning, Y.,Kawano, Y., and Wang, GL. (2015) The RhoGAP SPIN6 Associates with SPL11 and OsRac1 and Negatively Regulates Programmed Cell Death and Innate Immunity in Rice. PLoS Pathog. 11:e1004629. 2014

Kawano, Y. (Corresponding author), Kawano-Kaneko, T., and Shimamoto, K. (2014) Rho family GTPase-dependent immunity in plants and animals. Front. Plant Sci. 5:522

Kawano, Y. (Corresponding author), Fujiwara, T., Yao, A., Housen, Y., Hayashi, K., and Shimamoto, K. Palmitoylation-dependent membrane localization of the rice R protein Pit is critical for the activation of the small GTPase OsRac1. J Biol Chem. 2014 289:19079-88

Césari, S., Kanzaki, H., Fujiwara, T., Bernoux, M., Chalvon, V., Kawano, Y., Shimamoto, K., Dodds, P., Terauchi, R. Kroj, T., The NB-LRR proteins RGA4 and RGA5 interact functionally and physically to confer disease resistance. EMBO J. In press

Kosami, K, Ohki, I., Nagano,M., Furuita, K., Sugiki, T., Kawano, Y., Kawasaki,Y., Fujiwara, T., Nakagawa, A., Shimamoto, K., and Kojima, C. The crystal structure of the plant small GTPase OsRac1 reveals its mode of binding to NADPH oxidase. J Biol Chem. In press

Sakane, H., Horii, Y, Nogami, S., Kawano, Y., Kaneko-Kawano, T., and Shirataki, H. (2014) α-Taxilin forms a complex with sorting nexin 4 and participates in the recycling pathway of transferrin receptor. PLoS One 9, e93509 2012

2013
Kawano, Y., and Shimamoto, K. (2013) Early signaling network in rice PRR- and R-mediated immunity. Curr Opin Plant Biol. 16: 496-504

Dang, TT. Shimatani, Z., Kawano, Y. (Corresponding author), Terada, R and Shimamoto, K. (2013) Gene editing a constitutively active OsRac1 by homologous recombination-based gene targeting induces immune responses in rice Plant Cell Physiol 54, 2058-2070

Akamatsu, A., Wong, H., Fujiwara, M., Okuda, J., Nishide, K., Uno, K., Imai, K., Umemura, K., Kawasaki, T., Kawano, Y., and Shimamoto, K. (2013) An OsCEBiP/OsCERK1-OsRacGEF1-OsRac1 module is an essential component of chitin-induced rice immunity. Cell Host Microbe 13, 465-476

2012
Kim, S. H., Oikawa, T., Kyozuka, J., Wong, H. L., Umemura, K., Kishi-Kaboshi, M., Takahashi, A., Kawano, Y., Kawasaki, T., and Shimamoto, K. (2012) The bHLH Rac immunity1 (RAI1) is activated by OsRac1 via OsMAPK3 and OsMAPK6 in rice immunity. Plant Cell Physiol 53, 740-754

Wamaitha, M., Yamamoto, R., Wong, H., Kawasaki, T., Kawano, Y., and Shimamoto, K. (2012) OsRap2.6 transcription factor contributes to rice innate immunity through its interaction with Receptor for Activated Kinase-C 1 (RACK1). Rice 5, 35

Kaneko-Kawano, T., Takasu, F., Naoki, H., Sakumura, Y., Ishii, S., Ueba, T., Eiyama, A., Okada, A., Kawano, Y., and Suzuki, K. (2012) Dynamic regulation of myosin light chain phosphorylation by Rho-kinase. PLoS One 7, e39269

Horii, Y., Nogami, S., Kawano, Y., Kaneko-Kawano, T., Ohtomo, N., Tomiya, T., and Shirataki, H. (2012) Interaction of alpha-taxilin localized on intracellular components with the microtubule cytoskeleton. Cell Struct Funct 37, 111-126

Kawano, Y., Akamatsu, A., Hayashi, K., Housen, Y., Okuda, J., Yao, A., Nakashima, A., Takahashi, H., Yoshida, H., Wong, H. L., Kawasaki, T., and Shimamoto, K. (2010a) Activation of a Rac GTPase by the NLR family disease resistance protein Pit plays a critical role in rice innate immunity. Cell Host Microbe 7, 362-375

Kawano, Y., Chen, L., and Shimamoto, K. (2010b) The function of Rac small GTPase and associated proteins in rice innate immunity. Rice 3, 112-121

Kawasaki T, Imai K, Wong H, Kawano Y, Nishide K, Okuda J, and Shimamoto K. Rice guanine nucleotide exchange factors for small GTPase OsRac1 involved in innate immunity of rice. In Advances in Genetics, Genomics and Control of Rice Blast Disease. 179-184, 2009

Yoshimura, T., Arimura, N., Kawano, Y., Kawabata, S., Wang, S., and Kaibuchi, K. (2006) Ras regulates neuronal polarity via the PI3-kinase/Akt/GSK-3beta/CRMP-2 pathway. Biochem Biophys Res Commun 340, 62-68

Kawano, Y., Yoshimura, T., Tsuboi, D., Kawabata, S., Kaneko-Kawano, T., Shirataki, H., Takenawa, T., and Kaibuchi, K. (2005) CRMP-2 is involved in kinesin-1-dependent transport of the Sra-1/WAVE1 complex and axon formation. Mol Cell Biol 25, 9920-9935

Kawano, Y., Kaneko, T., Yoshimura, T., Kawabata, S., and Kaibuchi, K. (2005) RhoA/C and the Actin Cytoskeleton. RHO Family GTPases, 113-136

Yoshimura, T., Kawano, Y., Arimura, N., Kawabata, S., Kikuchi, A., and Kaibuchi, K. (2005) GSK-3beta regulates phosphorylation of CRMP-2 and neuronal polarity. Cell 120, 137-149

Arimura, N., Menager, C., Kawano, Y., Yoshimura, T., Kawabata, S., Hattori, A., Fukata, Y., Amano, M., Goshima, Y., Inagaki, M., Morone, N., Usukura, J., and Kaibuchi, K. (2005) Phosphorylation by Rho kinase regulates CRMP-2 activity in growth cones. Mol Cell Biol 25, 9973-9984

Kaneko, T., Maeda, A., Takefuji, M., Aoyama, H., Nakayama, M., Kawabata, S., Kawano, Y., Iwamatsu, A., Amano, M., and Kaibuchi, K. (2005) Rho mediates endocytosis of epidermal growth factor receptor through phosphorylation of endophilin A1 by Rho-kinase. Genes Cells 10, 973-98

Kawano, Y., Yoshimura, T., and Kaibuchi, K. (2002) Smooth muscle contraction by small GTPase Rho. Nagoya J Med Sci 65, 1-8

Inagaki, N., Chihara, K., Arimura, N., Menager, C., Kawano, Y., Matsuo, N., Nishimura, T., Amano, M., and Kaibuchi, K. (2001) CRMP-2 induces axons in cultured hippocampal neurons. Nat Neurosci 4, 781-782

Kandabashi, T., Shimokawa, H., Miyata, K., Kunihiro, I., Kawano, Y., Fukata, Y., Higo, T., Egashira, K., Takahashi, S., Kaibuchi, K., and Takeshita, A. (2000) Inhibition of myosin phosphatase by upregulated rho-kinase plays a key role for coronary artery spasm in a porcine model with interleukin-1beta. Circulation 101, 1319-1323

Kawano, Y., Fukata, Y., Oshiro, N., Amano, M., Nakamura, T., Ito, M., Matsumura, F., Inagaki, M., and Kaibuchi, K. (1999) Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo. J Cell Biol 147, 1023-1038

Fukata, Y., Oshiro, N., Kinoshita, N., Kawano, Y., Matsuoka, Y., Bennett, V., Matsuura, Y., and Kaibuchi, K. (1999) Phosphorylation of adducin by Rho-kinase plays a crucial role in cell motility. J Cell Biol 145, 347-361

26.Yamamoto, T., Harada, N., Kawano, Y., Taya, S., and Kaibuchi, K. (1999) In vivo interaction of AF-6 with activated Ras and ZO-1. Biochem Biophys Res Commun 259, 103-107

Taya, S., Yamamoto, T., Kano, K., Kawano, Y., Iwamatsu, A., Tsuchiya, T., Tanaka, K., Kanai-Azuma, M., Wood, S. A., Mattick, J. S., and Kaibuchi, K. (1998) The Ras target AF-6 is a substrate of the fam deubiquitinating enzyme. J Cell Biol 142, 1053-1062