Faculty Profiles - KAWANO Youji

Papers - KAWANO Youji

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Stem Cell Factors BAM1 and WOX1 Suppressing Longitudinal Cell Division of Margin Cells Evoked by Low-Concentration Auxin in Young Cotyledon of Arabidopsis

Yuli Jiang, Jian Liang, Chunyan Wang, Li Tan, Yoji Kawano, Shingo Nagawa

International Journal of Molecular Sciences 26 ( 10 ) 4724 - 4724 2025.5

Publishing type：Research paper (scientific journal) Publisher：MDPI AG

Highly differentiated tissues and organs play essential biological functions in multicellular organisms. Coordination of organ developmental process with tissue differentiation is necessary to achieve proper development of mature organs, but mechanisms for such coordination are not well understood. We used cotyledon margin cells from Arabidopsis plant as a new model system to investigate cell elongation and cell division during organ growth and found that margin cells endured a developmental phase transition from the “elongation” phase to the “elongation and division” phase at the early stage in germinating seedlings. We also discovered that the stem cell factors BARELY ANY MERISTEM 1 (BAM1) and WUSCHEL-related homeobox1 (WOX1) are involved in the regulation of margin cell developmental phase transition. Furthermore, exogenous auxin treatment (1 nanomolar,nM) promotes cell division, especially longitudinal cell division. This promotion of cell division did not occur in bam1 and wox1 mutants. Based on these findings, we hypothesized a new “moderate auxin concentration” model which emphasizes that a moderate auxin concentration is the key to triggering the developmental transition of meristematic cells.

DOI： 10.3390/ijms26104724

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A PRA-Rab trafficking machinery modulates NLR immune receptor plasma membrane microdomain anchoring and blast resistance in rice Reviewed

Di Liang, Dongyong Yang, Tai Li, Zhe Zhu, Bingxiao Yan, Yang He, Xiaoyuan Li, Keran Zhai, Jiyun Liu, Yoji Kawano, Yiwen Deng, Xu Na Wu, Junzhong Liu, Zuhua He

Science Bulletin 2025.3

The mutual regulation between the pattern recognition receptor OsCERK1 and the E3 ubiquitin ligase OsCIE1 controls induction and homeostasis of immunity Reviewed

Qiong Wang, Yoji Kawano

Science Bulletin 2024.7

An NLR paralog Pit2 generated from tandem duplication of Pit1 fine-tunes Pit1 localization and function. Reviewed International journal

Yuying Li, Qiong Wang, Huimin Jia, Kazuya Ishikawa, Ken-Ichi Kosami, Takahiro Ueba, Atsumi Tsujimoto, Miki Yamanaka, Yasuyuki Yabumoto, Daisuke Miki, Eriko Sasaki, Yoichiro Fukao, Masayuki Fujiwara, Takako Kaneko-Kawano, Li Tan, Chojiro Kojima, Rod A Wing, Alfino Sebastian, Hideki Nishimura, Fumi Fukada, Qingfeng Niu, Motoki Shimizu, Kentaro Yoshida, Ryohei Terauchi, Ko Shimamoto, Yoji Kawano

Nature Communications 15 ( 1 ) 4610 - 4610 2024.5

Authorship：Last author,　Corresponding author Language：English Publishing type：Research paper (scientific journal)

NLR family proteins act as intracellular receptors. Gene duplication amplifies the number of NLR genes, and subsequent mutations occasionally provide modifications to the second gene that benefits immunity. However, evolutionary processes after gene duplication and functional relationships between duplicated NLRs remain largely unclear. Here, we report that the rice NLR protein Pit1 is associated with its paralogue Pit2. The two are required for the resistance to rice blast fungus but have different functions: Pit1 induces cell death, while Pit2 competitively suppresses Pit1-mediated cell death. During evolution, the suppression of Pit1 by Pit2 was probably generated through positive selection on two fate-determining residues in the NB-ARC domain of Pit2, which account for functional differences between Pit1 and Pit2. Consequently, Pit2 lost its plasma membrane localization but acquired a new function to interfere with Pit1 in the cytosol. These findings illuminate the evolutionary trajectory of tandemly duplicated NLR genes after gene duplication.

DOI： 10.1038/s41467-024-48943-5

PubMed

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The secreted immune response peptide 1 functions as a phytocytokine in rice immunity Reviewed

Pingyu Wang, Huimin Jia, Ting Guo, Yuanyuan Zhang, Wanqing Wang, Hideki Nishimura, Zhengguo Li, Yoji Kawano

Journal of Experimental Botany 74 ( 3 ) 1059 - 1073 2023.2

Authorship：Last author,　Corresponding author Publishing type：Research paper (scientific journal) Publisher：Oxford University Press (OUP)

Abstract

Small signalling peptides play important roles in various plant processes, but information regarding their involvement in plant immunity is limited. We previously identified a novel small secreted protein in rice, called immune response peptide 1 (IRP1). Here, we studied the function of IRP1 in rice immunity. Rice plants overexpressing IRP1 enhanced resistance to the virulent rice blast fungus. Application of synthetic IRP1 to rice suspension cells triggered the expression of IRP1 itself and the defence gene phenylalanine ammonia-lyase 1 (PAL1). RNA-seq results revealed that 84% of genes up-regulated by IRP1, including 13 OsWRKY transcription factors, were also induced by a microbe-associated molecular pattern (MAMP), chitin, indicating that IRP1 and chitin share a similar signalling pathway. Co-treatment with chitin and IRP1 elevated the expression level of PAL1 and OsWRKYs in an additive manner. The increased chitin concentration arrested the induction of IRP1 and PAL1 expression by IRP1, but did not affect IRP1-triggered mitogen-activated protein kinases (MAPKs) activation. Collectively, our findings indicate that IRP1 functions as a phytocytokine in rice immunity regulating MAPKs and OsWRKYs that can amplify chitin and other signalling pathways, and provide new insights into how MAMPs and phytocytokines cooperatively regulate rice immunity.

DOI： 10.1093/jxb/erac455

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Other Link： https://academic.oup.com/jxb/article-pdf/74/3/1059/49092088/erac455.pdf

Improving disease resistance to rice false smut without yield penalty by manipulating the expression of effector target Reviewed

Qiong Wang, Yoji Kawano

Molecular Plant 15 ( 12 ) 1834 - 1837 2022.12

Three highly conserved hydrophobic residues in the predicted α2‐helix of rice NLR protein Pit contribute to its localization and immune induction Reviewed International journal

Qiong Wang, Yuying Li, Ken‐ichi Kosami, Chaochao Liu, Jing Li, Dan Zhang, Daisuke Miki, Yoji Kawano

Plant, Cell & Environment 45 ( 6 ) 1876 - 1890 2022.6

Authorship：Last author,　Corresponding author Language：English Publishing type：Research paper (scientific journal) Publisher：Wiley

Nucleotide-binding leucine-rich repeat (NLR) proteins work as crucial intracellular immune receptors. N-terminal domains of NLRs fall into two groups, coiled-coil (CC) and Toll-interleukin 1 receptor domains, which play critical roles in signal transduction and disease resistance. However, the activation mechanisms of NLRs, and how their N-termini function in immune induction, remain largely unknown. Here, we revealed that the CC domain of a rice NLR Pit contributes to self-association. The Pit CC domain possesses three conserved hydrophobic residues that are known to be involved in oligomer formation in two NLRs, barley MLA10 and Arabidopsis RPM1. Interestingly, the function of these residues in Pit differs from that in MLA10 and RPM1. Although three hydrophobic residues are important for Pit-induced disease resistance against rice blast fungus, they do not participate in self-association or binding to downstream signalling molecules. By homology modelling of Pit using the Arabidopsis ZAR1 structure, we tried to clarify the role of three conserved hydrophobic residues and found that they are located in the predicted α2-helix of the Pit CC domain and involved in the plasma membrane localization. Our findings provide novel insights for understanding the mechanisms of NLR activation as well as the relationship between subcellular localization and immune induction.

DOI： 10.1111/pce.14315

PubMed

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Other Link： https://onlinelibrary.wiley.com/doi/full-xml/10.1111/pce.14315

Fine-tuning ROS homeostasis by ROD1 is a battleground between rice and Magnaporthe oryzae Reviewed

Yoji Kawano

Molecular Plant 14 ( 12 ) 1979 - 1981 2021.12

NB-LRR-encoding genes conferring susceptibility to organophosphate pesticides in sorghum Reviewed

Zihuan Jing, Fiona Wacera W., Tsuneaki Takami, Hideki Takanashi, Fumi Fukada, Yoji Kawano, Hiromi Kajiya-Kanegae, Hiroyoshi Iwata, Nobuhiro Tsutsumi, Wataru Sakamoto

Scientific Reports 11 ( 1 ) 2021.12

Publishing type：Research paper (scientific journal) Publisher：Springer Science and Business Media LLC

<title>Abstract</title>Organophosphate is the commonly used pesticide to control pest outbreak, such as those by aphids in many crops. Despite its wide use, however, necrotic lesion and/or cell death following the application of organophosphate pesticides has been reported to occur in several species. To understand this phenomenon, called organophosphate pesticide sensitivity (OPS) in sorghum, we conducted QTL analysis in a recombinant inbred line derived from the Japanese cultivar NOG, which exhibits OPS. Mapping OPS in this population identified a prominent QTL on chromosome 5, which corresponded to <italic>Organophosphate-Sensitive Reaction</italic> (<italic>OSR</italic>) reported previously in other mapping populations. The <italic>OSR</italic> locus included a cluster of three genes potentially encoding nucleotide-binding leucine-rich repeat (NB-LRR, NLR) proteins, among which <italic>NLR-C</italic> was considered to be responsible for OPS in a dominant fashion. <italic>NLR-C</italic> was functional in NOG, whereas the other resistant parent, BTx623, had a null mutation caused by the deletion of promoter sequences. Our finding of <italic>OSR</italic> as a dominant trait is important not only in understanding the diversified role of NB-LRR proteins in cereals but also in securing sorghum breeding free from OPS.

DOI： 10.1038/s41598-021-98908-7

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Other Link： https://www.nature.com/articles/s41598-021-98908-7

The Small GTPase OsRac1 Forms Two Distinct Immune Receptor Complexes Containing the PRR OsCERK1 and the NLR Pit Reviewed

Akira Akamatsu, Masayuki Fujiwara, Satoshi Hamada, Megumi Wakabayashi, A i Yao, Qiong Wang, Ken-ichi Kosami, Thu Thi Dang, Takako Kaneko-Kawano, Fumi Fukada, K o Shimamoto, Yoji Kawano

Plant and Cell Physiology 62 ( 11 ) 1662 - 1675 2021.8

Authorship：Last author,　Corresponding author Publishing type：Research paper (scientific journal) Publisher：Oxford University Press (OUP)

<title>Abstract</title>
Plants employ two different types of immune receptors, cell surface pattern recognition receptors (PRRs) and intracellular nucleotide-binding and leucine-rich repeat-containing proteins (NLRs), to cope with pathogen invasion. Both immune receptors often share similar downstream components and responses but it remains unknown whether a PRR and an NLR assemble into the same protein complex or two distinct receptor complexes. We have previously found that the small GTPase OsRac1 plays key roles in the signaling of OsCERK1, a PRR for fungal chitin, and of Pit, an NLR for rice blast fungus, and associates directly and indirectly with both of these immune receptors. In this study, using biochemical and bioimaging approaches, we revealed that OsRac1 formed two distinct receptor complexes with OsCERK1 and with Pit. Supporting this result, OsCERK1 and Pit utilized different transport systems for anchorage to the plasma membrane (PM). Activation of OsCERK1 and Pit led to OsRac1 activation and, concomitantly, OsRac1 shifted from a small to a large protein complex fraction. We also found that the chaperone Hsp90 contributed to the proper transport of Pit to the PM and the immune induction of Pit. These findings illuminate how the PRR OsCERK1 and the NLR Pit orchestrate rice immunity through the small GTPase OsRac1.

DOI： 10.1093/pcp/pcab121

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Identification of endogenous small peptides involved in rice immunity through transcriptomics‐ and proteomics‐based screening Reviewed

Pingyu Wang, Shaolun Yao, Ken‐ichi Kosami, Ting Guo, Jing Li, Yuanyuan Zhang, Yoichiro Fukao, Takako Kaneko‐Kawano, Heng Zhang, Yi‐Min She, Pengcheng Wang, Weiman Xing, Kousuke Hanada, Renyi Liu, Yoji Kawano

Plant Biotechnology Journal 18 ( 2 ) 415 - 428 2020.2

In vivo monitoring of plant small GTPase activation using a Förster resonance energy transfer biosensor Reviewed International journal

Hann Ling Wong, Akira Akamatsu, Qiong Wang, Masayuki Higuchi, Tomonori Matsuda, Jun Okuda, Ken-ichi Kosami, Noriko Inada, Tsutomu Kawasaki, Takako Kaneko-Kawano, Shingo Nagawa, Li Tan, Yoji Kawano, Ko Shimamoto

Plant Methods 14 ( 1 ) 56 - 56 2018.12

Authorship：Corresponding author Language：English Publishing type：Research paper (scientific journal) Publisher：Springer Science and Business Media LLC

Background: Small GTPases act as molecular switches that regulate various plant responses such as disease resistance, pollen tube growth, root hair development, cell wall patterning and hormone responses. Thus, to monitor their activation status within plant cells is believed to be the key step in understanding their roles. Results: We have established a plant version of a Förster resonance energy transfer (FRET) probe called Ras and interacting protein chimeric unit (Raichu) that can successfully monitor activation of the rice small GTPase OsRac1 during various defence responses in cells. Here, we describe the protocol for visualizing spatiotemporal activity of plant Rac/ROP GTPase in living plant cells, transfection of rice protoplasts with Raichu-OsRac1 and acquisition of FRET images. Conclusions: Our protocol should be adaptable for monitoring activation for other plant small GTPases and protein-protein interactions for other FRET sensors in various plant cells.

DOI： 10.1186/s13007-018-0325-4

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Other Link： http://link.springer.com/article/10.1186/s13007-018-0325-4/fulltext.html

Resistance protein Pit interacts with the GEF OsSPK1 to activate OsRac1 and trigger rice immunity Reviewed

Qiong Wang, Yuying Li, Kazuya Ishikawa, Ken-ichi Kosami, Kazumi Uno, Shingo Nagawa, Li Tan, Jiamu Du, Ko Shimamoto, Yoji Kawano

Proceedings of the National Academy of Sciences 201813058 2018.11

The Intronic cis Element SE1 Recruits trans-Acting Repressor Complexes to Repress the Expression of ELONGATED UPPERMOST INTERNODE1 in Rice Reviewed

Yongyao Xie, Yaling Zhang, Jingluan Han, Jikai Luo, Gousi Li, Jianle Huang, Haibin Wu, Qingwei Tian, Qinlong Zhu, Yuanling Chen, Yoji Kawano, Yao-Guang Liu, Letian Chen

Molecular Plant 11 ( 5 ) 720 - 735 2018.5

Plasma Membrane Microdomains Are Essential for Rac1-RbohB/H-Mediated Immunity in Rice Reviewed International journal

Minoru Nagano, Toshiki Ishikawa, Masayuki Fujiwara, Yoichiro Fukao, Yoji Kawano, Maki Kawai-Yamada, Ko Shimamoto

The Plant Cell 28 ( 8 ) 1966 - 1983 2016.8

Language：English Publishing type：Research paper (scientific journal) Publisher：Oxford University Press (OUP)

<title>Abstract</title>
Numerous plant defense-related proteins are thought to congregate in plasma membrane microdomains, which consist mainly of sphingolipids and sterols. However, the extent to which microdomains contribute to defense responses in plants is unclear. To elucidate the relationship between microdomains and innate immunity in rice (Oryza sativa), we established lines in which the levels of sphingolipids containing 2-hydroxy fatty acids were decreased by knocking down two genes encoding fatty acid 2-hydroxylases (FAH1 and FAH2) and demonstrated that microdomains were less abundant in these lines. By testing these lines in a pathogen infection assay, we revealed that microdomains play an important role in the resistance to rice blast fungus infection. To illuminate the mechanism by which microdomains regulate immunity, we evaluated changes in protein composition, revealing that microdomains are required for the dynamics of the Rac/ROP small GTPase Rac1 and respiratory burst oxidase homologs (Rbohs) in response to chitin elicitor. Furthermore, FAHs are essential for the production of reactive oxygen species (ROS) after chitin treatment. Together with the observation that RbohB, a defense-related NADPH oxidase that interacts with Rac1, is localized in microdomains, our data indicate that microdomains are required for chitin-induced immunity through ROS signaling mediated by the Rac1-RbohB pathway.

DOI： 10.1105/tpc.16.00201

PubMed

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Crosstalk of Signaling Mechanisms Involved in Host Defense and Symbiosis Against Microorganisms in Rice Reviewed

Akira Akamatsu, Ko Shimamoto, Yoji Kawano

CURRENT GENOMICS 17 ( 4 ) 297 - 307 2016

The RhoGAP SPIN6 Associates with SPL11 and OsRac1 and Negatively Regulates Programmed Cell Death and Innate Immunity in Rice Reviewed

Jinling Liu, Chan Ho Park, Feng He, Minoru Nagano, Mo Wang, Maria Bellizzi, Kai Zhang, Xiaoshan Zeng, Wende Liu, Yuese Ning, Yoji Kawano, Guo-Liang Wang

PLOS PATHOGENS 11 ( 2 ) 2015.2

New insights into the dimerization of small GTPase Rac/ROP guanine nucleotide exchange factors in rice. Reviewed International journal

Akamatsu Akira, Uno Kazumi, Kato Midori, Wong Hann Ling, Shimamoto Ko, Kawano Yoji

Plant signaling & behavior 10 ( 7 ) e1044702 2015

Authorship：Last author,　Corresponding author Language：English Publishing type：Research paper (scientific journal)

Molecular links between receptor-kinases and Rac/ROP family small GTPases mediated by activator guanine nucleotide exchange factors (GEFs) govern diverse biological processes. However, it is unclear how the Rac/ROP GTPases orchestrate such a wide variety of activities. Here, we show that rice OsRacGEF1 forms homodimers, and heterodimers with OsRacGEF2, at the plasma membrane (PM) and the endoplasmic reticulum (ER). OsRacGEF2 does not bind directly to the receptor-like kinase (RLK) OsCERK1, but forms a complex with OsCERK1 through OsRacGEF1 at the ER. This complex is transported from ER to the PM and there associates with OsRac1, resulting in the formation of a stable immune complex. Such RLK-GEF heterodimer complexes may explain the diversity of Rac/ROP family GTPase signalings.

DOI： 10.1080/15592324.2015.1044702

PubMed

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Other Link： http://orcid.org/0000-0003-0687-2777

The Crystal Structure of the Plant Small GTPase OsRac1 Reveals Its Mode of Binding to NADPH Oxidase Reviewed

Ken-ichi Kosami, Izuru Ohki, Minoru Nagano, Kyoko Furuita, Toshihiko Sugiki, Yoji Kawano, Tsutomu Kawasaki, Toshimichi Fujiwara, Atsushi Nakagawa, Ko Shimamoto, Chojiro Kojima

JOURNAL OF BIOLOGICAL CHEMISTRY 289 ( 41 ) 28569 - 28578 2014.10

Rho family GTPase-dependent immunity in plants and animals Reviewed

Yoji Kawano, Takako Kaneko-Kawano, Ko Shimamoto

FRONTIERS IN PLANT SCIENCE 5 2014.10

The NB-LRR proteins RGA4 and RGA5 interact functionally and physically to confer disease resistance Reviewed

Stella Cesari, Hiroyuki Kanzaki, Tadashi Fujiwara, Maud Bernoux, Veronique Chalvon, Yoji Kawano, Ko Shimamoto, Peter Dodds, Ryohei Terauchi, Thomas Kroj

EMBO JOURNAL 33 ( 17 ) 1941 - 1959 2014.9

Palmitoylation-dependent Membrane Localization of the Rice Resistance Protein Pit Is Critical for the Activation of the Small GTPase OsRac1 Reviewed

Yoji Kawano, Tadashi Fujiwara, Ai Yao, Yusuke Housen, Keiko Hayashi, Ko Shimamoto

JOURNAL OF BIOLOGICAL CHEMISTRY 289 ( 27 ) 19079 - 19088 2014.7

alpha-Taxilin Interacts with Sorting Nexin 4 and Participates in the Recycling Pathway of Transferrin Receptor Reviewed

Hiroshi Sakane, Yukimi Horii, Satoru Nogami, Yoji Kawano, Takako Kaneko-Kawano, Hiromichi Shirataki

PLOS ONE 9 ( 4 ) e93509 2014.4

Gene Editing a Constitutively Active OsRac1 by Homologous Recombination-Based Gene Targeting Induces Immune Responses in Rice Reviewed

Thu Thi Dang, Zenpei Shimatani, Yoji Kawano, Rie Terada, Ko Shimamoto

PLANT AND CELL PHYSIOLOGY 54 ( 12 ) 2058 - 2070 2013.12

Early signaling network in rice PRR-mediated and R-mediated immunity Reviewed

Yoji Kawano, Ko Shimamoto

CURRENT OPINION IN PLANT BIOLOGY 16 ( 4 ) 496 - 504 2013.8

An OsCEBiP/OsCERK1-OsRacGEF1-OsRac1 Module Is an Essential Early Component of Chitin-Induced Rice Immunity Reviewed

Akira Akamatsu, Hann Lin Wong, Masayuki Fujiwara, Jun Okuda, Keita Nishide, Kazumi Uno, Keiko Imai, Kenji Umemura, Tsutomu Kawasaki, Yoji Kawano, Ko Shimamoto

CELL HOST & MICROBE 13 ( 4 ) 465 - 476 2013.4

OsRap2.6 transcription factor contributes to rice innate immunity through its interaction with Receptor for Activated Kinase-C 1 (RACK1) Reviewed

Mwathi Jane Wamaitha, Risa Yamamoto, Hann Ling Wong, Tsutomu Kawasaki, Yoji Kawano, Ko Shimamoto

RICE 5 ( 1 ) 35 2012.12

Dynamic Regulation of Myosin Light Chain Phosphorylation by Rho-kinase Reviewed

Takako Kaneko-Kawano, Fugo Takasu, Honda Naoki, Yuichi Sakumura, Shin Ishii, Takahiro Ueba, Akinori Eiyama, Aiko Okada, Yoji Kawano, Kenji Suzuki

PLOS ONE 7 ( 6 ) 2012.6

The bHLH Rac Immunity1 (RAI1) Is Activated by OsRac1 via OsMAPK3 and OsMAPK6 in Rice Immunity Reviewed

Sung-Hyun Kim, Tetsuo Oikawa, Junko Kyozuka, Hann Ling Wong, Kenji Umemura, Mitsuko Kishi-Kaboshi, Akira Takahashi, Yoji Kawano, Tsutomu Kawasaki, Ko Shimamoto

PLANT AND CELL PHYSIOLOGY 53 ( 4 ) 740 - 754 2012.4

Interaction of alpha-taxilin Localized on Intracellular Components with the Microtubule Cytoskeleton Reviewed

Yukimi Horii, Satoru Nogami, Yoji Kawano, Takako Kaneko-Kawano, Natsuko Ohtomo, Tomoaki Tomiya, Hiromichi Shirataki

CELL STRUCTURE AND FUNCTION 37 ( 2 ) 111 - 126 2012

The Function of Rac Small GTPase and Associated Proteins in Rice Innate Immunity Reviewed

Yoji Kawano, Letian Chen, Ko Shimamoto

RICE 3 ( 2-3 ) 112 - 121 2010.9

Activation of a Rac GTPase by the NLR Family Disease Resistance Protein Pit Plays a Critical Role in Rice Innate Immunity Reviewed

Yoji Kawano, Akira Akamatsu, Keiko Hayashi, Yusuke Housen, Jun Okuda, Ai Yao, Ayako Nakashima, Hiroki Takahashi, Hitoshi Yoshida, Hann Ling Wong, Tsutomu Kawasaki, Ko Shimamoto

CELL HOST & MICROBE 7 ( 5 ) 362 - 375 2010.5

Rice Guanine Nucleotide Exchange Factors for Small GTPase OsRac1 Involved in Innate Immunity of Rice Reviewed

Tsutomu Kawasaki, Keiko Imai, Hann Ling Wong, Yoji Kawano, Keita Nishide, Jun Okuda, Ko Shimamoto

ADVANCES IN GENETICS, GENOMICS AND CONTROL OF RICE BLAST DISEASE 179 - + 2009

Ras regulates neuronal polarity via the PI3-kinase/Akt/GSK-3 beta/CRMP-2 pathway Reviewed

T Yoshimura, N Arimura, Y Kawano, S Kawabata, SJ Wang, K Kaibuchi

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 340 ( 1 ) 62 - 68 2006.2

Phosphorylation by Rho kinase regulates CRMP-2 activity in growth cones Reviewed

N Arimura, C Menager, Y Kawano, T Yoshimura, S Kawabata, A Hattori, Y Fukata, M Amano, Y Goshima, M Inagaki, N Morone, J Usukura, K Kaibuchi

MOLECULAR AND CELLULAR BIOLOGY 25 ( 22 ) 9973 - 9984 2005.11

CRMP-2 is involved in kinesin-1-dependent transport of the Sra-1/WAVE1 complex and axon formation Reviewed

Y Kawano, T Yoshimura, D Tsuboi, S Kawabata, T Kaneko-Kawano, H Shirataki, T Takenawa, K Kaibuchi

MOLECULAR AND CELLULAR BIOLOGY 25 ( 22 ) 9920 - 9935 2005.11

Rho mediates endocytosis of epidermal growth factor receptor through phosphorylation of endophilin A1 by Rho-kinase Reviewed

T Kaneko, A Maeda, M Takefuji, H Aoyama, M Nakayama, S Kawabata, Y Kawano, A Iwamatsu, M Amano, K Kaibuchi

GENES TO CELLS 10 ( 10 ) 973 - 987 2005.10

Molecular mechanisms of neuronal polarity Reviewed

Takeshi Yoshimura, Yoji Kawano, Nariko Arimura, Saeko Kawabata, Kozo Kaibuchi

Japanese Journal of Neuropsychopharmacology 25 ( 4 ) 169 - 174 2005.8

GSK-3 beta regulates phosphorylation of CRMP-2 and neuronal polarity Reviewed

T Yoshimura, Y Kawano, N Arimura, S Kawabata, A Kikuchi, K Kaibuchi

CELL 120 ( 1 ) 137 - 149 2005.1

RhoA/C and the Actin Cytoskeleton. Invited Reviewed

Kawano Y, Kaneko-Kawano T, Yoshimura T, Kawabata S, Kaibuchi K

“Rho Family GTPases” 6 113 - 136 2005

Smooth muscle contraction by small GTPase Rho Reviewed

Kawano Y, Yoshimura T, Kaibuchi K

Nagoya J Med Sci 65 ( 1-2 ) 1 - 8 2002

CRMP-2 induces axons in cultured hippocampal neurons Reviewed

N Inagaki, K Chihara, N Arimura, C Menager, Y Kawano, N Matsuo, T Nishimura, M Amano, K Kaibuchi

NATURE NEUROSCIENCE 4 ( 8 ) 781 - 782 2001.8

Inhibition of myosin phosphatase by upregulated Rho-kinase plays a key role for coronary artery spasm in a porcine model with interleukin-1 beta Reviewed

T Kandabashi, H Shimokawa, K Miyata, Kunihiro, I, Y Kawano, Y Fukata, T Higo, K Egashira, S Takahashi, K Kaibuchi, A Takeshita

CIRCULATION 101 ( 11 ) 1319 - 1323 2000.3

Phosphorylation of myosin-binding subunit (MBS) of myosin phosphatase by Rho-kinase in vivo Reviewed

Y Kawano, Y Fukata, N Oshiro, M Amano, T Nakamura, M Ito, F Matsumura, M Inagaki, K Kaibuchi

JOURNAL OF CELL BIOLOGY 147 ( 5 ) 1023 - 1037 1999.11

In vivo interaction of AF-6 with activated Ras and ZO-1 Reviewed

T Yamamoto, N Harada, Y Kawano, S Taya, K Kaibuchi

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 259 ( 1 ) 103 - 107 1999.5

Phosphorylation of adducin by rho-kinase plays a crucial role in cell motility Reviewed

Y Fukata, N Oshiro, N Kinoshita, Y Kawano, Y Matsuoka, Bennett, V, Y Matsuura, K Kaibuchi

JOURNAL OF CELL BIOLOGY 145 ( 2 ) 347 - 361 1999.4

The Ras target AF-6 is a substrate of the Fam deubiquitinating enzyme Reviewed

S Taya, T Yamamoto, K Kano, Y Kawano, A Iwamatsu, T Tsuchiya, K Tanaka, M Kanai-Azuma, SA Wood, JS Mattick, K Kaibuchi

JOURNAL OF CELL BIOLOGY 142 ( 4 ) 1053 - 1062 1998.8

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Papers - KAWANO Youji