Research activity information

• Oct. 2018 Kobe University Shinryoku-kai, Young Investigator Award

  IMASAKI Tsuyoshi

• CAMSAP2 condensates drive a γ-TuRC-independent pathway for non-centrosomal microtubule nucleation

  Ayhan Yurtsever, Tsuyoshi Imasaki, Ryota Kitano, Kien Xuan Ngo, Tomoaki Yagi, Shuhei Kuno, Hanjin Liu, Takaaki Kato, Hideki Shigematsu, Md Fahim Newaz, Yuji Sugita, Takeshi Fukuma, Ryo Nitta

  Microtubule nucleation is commonly viewed as a γ-tubulin ring complex (γ-TuRC)-templated process, yet many differentiated cells build extensive non-centrosomal microtubule arrays of unclear origin. Although spontaneous tubulin nucleation has long been observed in vitro as a γ-TuRC-independent nucleation process, its mechanism and cellular relevance have remained unclear. Here we show that CAMSAP2, a microtubule minus-end-binding protein, links spontaneous nucleation to non-centrosomal microtubule organization. Cryo-electron microscopy (cryo-EM), high-speed atomic force microscopy (hsAFM), and molecular dynamics simulations reveal that CAMSAP2 lowers the nucleation barrier by straightening tubulin oligomers and promoting lateral protofilament interactions that drive sheet formation and closure into microtubules. hsAFM captures stepwise nucleation and early growth, revealing that tubulin rings can serve as productive intermediates rather than dead-end depolymerization products. CAMSAP2 further self-organizes through liquid-liquid phase separation (LLPS) to concentrate tubulin and assembly intermediates, thereby promoting efficient microtubule formation at non-centrosomal microtubule-organizing centers. In HeLa cells, dispersed CAMSAP2 condensates act as γ-TuRC-independent microtubule-organizing centers alongside centrosomal asters, supporting a model in which spontaneous nucleation contributes to non-centrosomal microtubule biogenesis.

  openRxiv, May 2026, bioRxiv


• Structural analysis of a motor with increased mechanical output reveals new transitions in kinesin microtubule motility

  Satoki Shibata, Matthew Y. Wang, Tsuyoshi Imasaki, Hideki Shigematsu, Diego Ugarte La Torre, Yuanyuan Wei, Chacko Jobichen, Hajime Hagio, J. Sivaraman, Yuji Sugita, Sharyn A. Endow, Ryo Nitta

  Springer Science and Business Media LLC, Jan. 2026, Scientific Reports, 16(1) (1)

  [Refereed]

  Scientific journal

  Link to Kobe Univ. Repository (Kernel)


• Human spastin functions as an ATPase-independent microtubule nucleator via ring-stack formation

  Hanjin Liu, Nao Matsumoto, Toshiyuki Kaneshiro, Takaaki Kato, Hideki Shigematsu, Satoshi Kikkawa, Eriko Nitta, Tsuyoshi Imasaki, Ryo Nitta

  Abstract Microtubule severing enzyme spastin plays pivotal roles in cytokinesis and neuronal outgrowth, and its mutations cause hereditary spastic paraplegia (HSP). Here we show that, at physiological tubulin concentrations, human spastin behaves predominantly as an ATPase- independent microtubule nucleator rather than a severase. Biochemical and structural analyses revealed that spastin assembles tubulin into stacked-ring intermediates via strategically positioned microtubule-binding domains, thereby generating nucleation-competent sites for polymerization. Tubulin subunits within these spastin-induced rings adopt a straight, microtubule-like interface, in marked contrast to the twisted tubulin spirals characteristic of depolymerizing microtubule ends. Our results redefine the mechanistic landscape of multifaceted spastin functions and provide insights that may inform the pathological basis of HSP and guide future therapeutic strategies.

  Cold Spring Harbor Laboratory, Nov. 2025, bioRxiv


• Enhanced axonal transport in large vertebrates: KIF5A adaptations in giraffes and pythons

  Taketoshi Kambara, Lu Rao, Yosuke Yamagishi, Kazuho Ikeda, Daisuke Taniguchi, Tsuyoshi Imasaki, Hideki Shigematsu, Naoki Sakai, Arne Gennerich, Ryo Nitta, Yasushi Okada

  May 2025, bioRxiv


• Cryo-ET of actin cytoskeleton and membrane structure in lamellipodia formation using optogenetics

  Hironori Inaba, Tsuyoshi Imasaki, Kazuhiro Aoyama, Shogo Yoshihara, Hiroko Takazaki, Takayuki Kato, Hidemasa Goto, Kaoru Mitsuoka, Ryo Nitta, Takao Nakata

  Apr. 2025, iScience

  [Refereed]

  Scientific journal


• Dimerization of GAS2 mediates crosslinking of microtubules and F-actin

  Jiancheng An, Tsuyoshi Imasaki, Akihiro Narita, Shinsuke Niwa, Ryohei Sasaki, Tsukasa Makino, Ryo Nitta, Masahide Kikkawa

  Abstract The spectraplakin family protein GAS2 was originally identified as a growth arrest-specific protein, and recent studies have revealed its involvement in multiple cellular processes. Its dual interaction with actin filaments and microtubules highlights its essential role in cytoskeletal organization, such as cell division, apoptosis, and possibly tumorigenesis. However, the structural basis of cytoskeletal dynamics regulation by GAS2 remains unclear. In this study, we present cryo-electron microscopy structures of the GAS2 type 3 calponin homology domain (CH3) in complex with F-actin at 2.8 Å resolution, thus solving the first type CH3 domain structure bound to F-actin and confirming its actin-binding activity. We also provide the first near-atomic resolution cryo-EM structure of the GAS2-GAR domain bound to microtubules and identify conserved microtubule-binding residues. Our biochemical experiments show that GAS2 promotes microtubule nucleation and polymerization, and that its C-terminal region is essential for dimerization, bundling of both F-actin and microtubules, and microtubule nucleation. As mutations leading to expression of C-terminally truncated GAS2 have been linked to hearing loss, these findings suggest that the disruption of GAS2-dependent cytoskeletal organisation could underlie auditory dysfunction.

  Springer Science and Business Media LLC, Apr. 2025, The EMBO Journal

  [Refereed]

  Scientific journal


• Structural basis of Irgb6 inactivation by Toxoplasma gondii through the phosphorylation of switch

  Hiromichi Okuma, Yumiko Saijo‐Hamano, Hiroshi Yamada, Aalaa Alrahman Sherif, Emi Hashizaki, Naoki Sakai, Takaaki Kato, Tsuyoshi Imasaki, Satoshi Kikkawa, Eriko Nitta, Miwa Sasai, Tadashi Abe, Fuminori Sugihara, Yoshimasa Maniwa, Hidetaka Kosako, Kohji Takei, Daron M. Standley, Masahiro Yamamoto, Ryo Nitta

  Abstract Irgb6 is a priming immune‐related GTPase (IRG) that counteracts Toxoplasma gondii. It is known to be recruited to the low virulent type II T. gondii parasitophorous vacuole (PV), initiating cell‐autonomous immunity. However, the molecular mechanism by which immunity‐related GTPases become inactivated after the parasite infection remains obscure. Here, we found that Thr95 of Irgb6 is prominently phosphorylated in response to low virulent type II T. gondii infection. We observed that a phosphomimetic T95D mutation in Irgb6 impaired its localization to the PV and exhibited reduced GTPase activity in vitro. Structural analysis unveiled an atypical conformation of nucleotide‐free Irgb6‐T95D, resulting from a conformational change in the G‐domain that allosterically modified the PV membrane‐binding interface. In silico docking corroborated the disruption of the physiological membrane binding site. These findings provide novel insights into a T. gondii‐induced allosteric inactivation mechanism of Irgb6.

  Wiley, Nov. 2023, Genes to Cells

  [Refereed]

  Scientific journal

  Link to Kobe Univ. Repository (Kernel)


• TEAD1 trapping by the Q353R–Lamin A/C causes dilated cardiomyopathy

  Shintaro Yamada, Toshiyuki Ko, Masamichi Ito, Tatsuro Sassa, Seitaro Nomura, Hiromichi Okuma, Mayuko Sato, Tsuyoshi Imasaki, Satoshi Kikkawa, Bo Zhang, Takanobu Yamada, Yuka Seki, Kanna Fujita, Manami Katoh, Masayuki Kubota, Satoshi Hatsuse, Mikako Katagiri, Hiromu Hayashi, Momoko Hamano, Norifumi Takeda, Hiroyuki Morita, Shuji Takada, Masashi Toyoda, Masanobu Uchiyama, Masashi Ikeuchi, Kiminori Toyooka, Akihiro Umezawa, Yoshihiro Yamanishi, Ryo Nitta, Hiroyuki Aburatani, Issei Komuro

  Mutations in the LMNA gene encoding Lamin A and C (Lamin A/C), major components of the nuclear lamina, cause laminopathies including dilated cardiomyopathy (DCM), but the underlying molecular mechanisms have not been fully elucidated. Here, by leveraging single-cell RNA sequencing (RNA-seq), assay for transposase-accessible chromatin using sequencing (ATAC-seq), protein array, and electron microscopy analysis, we show that insufficient structural maturation of cardiomyocytes owing to trapping of transcription factor TEA domain transcription factor 1 (TEAD1) by mutant Lamin A/C at the nuclear membrane underlies the pathogenesis of Q353R -LMNA– related DCM. Inhibition of the Hippo pathway rescued the dysregulation of cardiac developmental genes by TEAD1 in LMNA mutant cardiomyocytes. Single-cell RNA-seq of cardiac tissues from patients with DCM with the LMNA mutation confirmed the dysregulated expression of TEAD1 target genes. Our results propose an intervention for transcriptional dysregulation as a potential treatment of LMNA -related DCM.

  American Association for the Advancement of Science (AAAS), Apr. 2023, Science Advances, 9(15) (15)

  [Refereed]

  Scientific journal

  Link to Kobe Univ. Repository (Kernel)


• Structural model of microtubule dynamics inhibition by kinesin-4 from the crystal structure of KLP-12 –tubulin complex

  Shinya Taguchi, Juri Nakano, Tsuyoshi Imasaki, Tomoki Kita, Yumiko Saijo-Hamano, Naoki Sakai, Hideki Shigematsu, Hiromichi Okuma, Takahiro Shimizu, Eriko Nitta, Satoshi Kikkawa, Satoshi Mizobuchi, Shinsuke Niwa, Ryo Nitta

  Abstract Kinesin superfamily proteins are microtubule-based molecular motors driven by the energy of ATP hydrolysis. Among them, the kinesin-4 family is a unique motor that inhibits microtubule dynamics. Although mutations of kinesin-4 cause several diseases, its molecular mechanism is unclear because of the difficulty of visualizing the high-resolution structure of kinesin-4 working at the microtubule plus-end. Here, we report that KLP-12, a C. elegans kinesin-4 ortholog of KIF21A and KIF21B, is essential for proper length control of C. elegans axons, and its motor domain represses microtubule polymerization in vitro. The crystal structure of the KLP-12 motor domain complexed with tubulin, which represents the high-resolution structural snapshot of inhibition state of microtubule-end dynamics, revealed the bending effect of KLP-12 for tubulin. Comparison with the KIF5B-tubulin and KIF2C-tubulin complexes, which represent the elongation and shrinking forms of microtubule ends, respectively, showed the curvature of tubulin introduced by KLP-12 is in between them. Taken together, KLP-12 controls the proper length of axons by modulating the curvature of the microtubule ends to inhibit the microtubule dynamics.

  Lead, Cold Spring Harbor Laboratory, Sep. 2022, eLife

  [Refereed]

  Scientific journal

  Link to Kobe Univ. Repository (Kernel)


• CAMSAP2 organizes a γ-tubulin-independent microtubule nucleation centre through phase separation.

  Tsuyoshi Imasaki, Satoshi Kikkawa, Shinsuke Niwa, Yumiko Saijo-Hamano, Hideki Shigematsu, Kazuhiro Aoyama, Kaoru Mitsuoka, Takahiro Shimizu, Mari Aoki, Ayako Sakamoto, Yuri Tomabechi, Naoki Sakai, Mikako Shirouzu, Shinya Taguchi, Yosuke Yamagishi, Tomiyoshi Setsu, Yoshiaki Sakihama, Eriko Nitta, Masatoshi Takeichi, Ryo Nitta

  Microtubules are dynamic polymers consisting of αβ-tubulin heterodimers. The initial polymerization process, called microtubule nucleation, occurs spontaneously via αβ-tubulin. Since a large energy barrier prevents microtubule nucleation in cells, the γ-tubulin ring complex is recruited to the centrosome to overcome the nucleation barrier. However, a considerable number of microtubules can polymerize independently of the centrosome in various cell types. Here, we present evidence that the minus-end-binding calmodulin-regulated spectrin-associated protein 2 (CAMSAP2) serves as a strong nucleator for microtubule formation by significantly reducing the nucleation barrier. CAMSAP2 co-condensates with αβ-tubulin via a phase separation process, producing plenty of nucleation intermediates. Microtubules then radiate from the co-condensates, resulting in aster-like structure formation. CAMSAP2 localizes at the co-condensates and decorates the radiating microtubule lattices to some extent. Taken together, these in vitro findings suggest that CAMSAP2 supports microtubule nucleation and growth by organizing a nucleation centre as well as by stabilizing microtubule intermediates and growing microtubules.

  Lead, Jun. 2022, eLife, 11, English, International magazine

  [Refereed]

  Scientific journal

  Link to Kobe Univ. Repository (Kernel)


• A practical method for efficient and optimal production of Seleno‐methionine‐labeled recombinant protein complexes in the insect cells

  Sabine Wenzel, Tsuyoshi Imasaki, Yuichiro Takagi

  Lead, Wiley, Apr. 2019, Protein Science, 28(4) (4), 808 - 822

  [Refereed]

  Scientific journal


• High-resolution crystal structure of human asparagine synthetase enables analysis of inhibitor binding and selectivity.

  Wen Zhu, Ashish Radadiya, Claudine Bisson, Sabine Wenzel, Brian E Nordin, Francisco Martínez-Márquez, Tsuyoshi Imasaki, Svetlana E Sedelnikova, Adriana Coricello, Patrick Baumann, Alexandria H Berry, Tyzoon K Nomanbhoy, John W Kozarich, Yi Jin, David W Rice, Yuichiro Takagi, Nigel G J Richards

  Expression of human asparagine synthetase (ASNS) promotes metastatic progression and tumor cell invasiveness in colorectal and breast cancer, presumably by altering cellular levels of L-asparagine. Human ASNS is therefore emerging as a bona fide drug target for cancer therapy. Here we show that a slow-onset, tight binding inhibitor, which exhibits nanomolar affinity for human ASNS in vitro, exhibits excellent selectivity at 10 μM concentration in HCT-116 cell lysates with almost no off-target binding. The high-resolution (1.85 Å) crystal structure of human ASNS has enabled us to identify a cluster of negatively charged side chains in the synthetase domain that plays a key role in inhibitor binding. Comparing this structure with those of evolutionarily related AMP-forming enzymes provides insights into intermolecular interactions that give rise to the observed binding selectivity. Our findings demonstrate the feasibility of developing second generation human ASNS inhibitors as lead compounds for the discovery of drugs against metastasis.

  2019, Communications biology, 2, 345 - 345, English, International magazine

  [Refereed]

  Scientific journal

  Link to Kobe Univ. Repository (Kernel)


• Structural insight into microtubule stabilization and kinesin inhibition by Tau family MAPs

  Hideki Shigematsu, Tsuyoshi Imasaki, Chihiro Doki, Takuya Sumi, Mari Aoki, Tomomi Uchikubo-Kamo, Ayako Sakamoto, Kiyotaka Tokuraku, Mikako Shirouzu, Ryo Nitta

  The Tau family microtubule-associated proteins (MAPs) promote microtubule stabilization and regulate microtubule-based motility. They share the C-terminal microtubule-binding domain, which includes three to five tubulin-binding repeats. Different numbers of repeats formed by alternative splicing have distinct effects on the activities of these proteins, and the distribution of these variants regulates fundamental physiological phenomena in cells. In this study, using cryo-EM, we visualized the MAP4 microtubule complex with the molecular motor kinesin-1. MAP4 bound to the C-terminal domains of tubulins along the protofilaments stabilizes the longitudinal contacts of the microtubule. The strongest bond of MAP4 was found around the intertubulin–dimer interface such that MAP4 coexists on the microtubule with kinesin-1 bound to the intratubulin–dimer interface as well. MAP4, consisting of five repeats, further folds and accumulates above the intertubulin–dimer interface, interfering with kinesin-1 movement. Therefore, these cryo-EM studies reveal new insight into the structural basis of microtubule stabilization and inhibition of kinesin motility by the Tau family MAPs.

  Lead, Rockefeller University Press, Dec. 2018, Journal of Cell Biology, 217(12) (12), 4155 - 4163

  [Refereed]

  Scientific journal

  Link to Kobe Univ. Repository (Kernel)


• Recent progress in structural biology: lessons from our research history.

  Nitta R, Imasaki T, Nitta E

  May 2018, Microscopy (Oxford, England)

  [Refereed]

  Link to Kobe Univ. Repository (Kernel)


• Titer estimation for quality control (TEQC) method: A practical approach for optimal production of protein complexes using the baculovirus expression vector system

  Tsuyoshi Imasaki, Sabine Wenzel, Kentaro Yamada, Megan L. Bryant, Yuichiro Takagi

  Lead, Public Library of Science, Apr. 2018, PLoS ONE, 13(4) (4), e0195356, English

  [Refereed]

  Scientific journal


• Structural insights into the altering function of CRMP2 by phosphorylation

  Takuya Sumi, Tsuyoshi Imasaki, Mari Aoki, Naoki Sakai, Eriko Nitta, Mikako Shirouzu, Ryo Nitta

  Japan Society for Cell Biology, Feb. 2018, Cell Structure and Function, 43(1) (1), 15 - 23, English

  [Refereed]

  Scientific journal

  Link to Kobe Univ. Repository (Kernel)


• Yeast Hrq1 shares structural and functional homology with the disease-linked human RecQ4 helicase

  Cody M. Rogers, Joseph Che-Yen Wang, Hiroki Noguchi, Tsuyoshi Imasaki, Yuichiro Takagi, Matthew L. Bochman

  May 2017, NUCLEIC ACIDS RESEARCH, 45(9) (9), 5217 - 5230, English

  [Refereed]

  Scientific journal


• Expression and purification of functional human glycogen synthase-1 (hGYS1) in insect cells

  May Khanna, Tsuyoshi Imasaki, Vimbai M. Chikwana, Samantha Perez-Miller, Gerald O. Hunter, Amber Mosley, Yuichiro Takagi, Thomas D. Hurley

  Aug. 2013, PROTEIN EXPRESSION AND PURIFICATION, 90(2) (2), 78 - 83, English

  [Refereed]

  Scientific journal


• Interaction of the Mediator Head Module with RNA Polymerase II

  Gang Cai, Yuriy L. Chaban, Tsuyoshi Imasaki, Julio A. Kovacs, Guillermo Calero, Pawel A. Penczek, Yuichiro Takagi, Francisco J. Asturias

  May 2012, STRUCTURE, 20(5) (5), 899 - 910, English

  [Refereed]

  Scientific journal


• MultiBac: expanding the research toolbox for multiprotein complexes

  Christoph Bieniossek, Tsuyoshi Imasaki, Yuichiro Takagi, Imre Berger

  Feb. 2012, TRENDS IN BIOCHEMICAL SCIENCES, 37(2) (2), 49 - 57, English

  [Refereed]


• Substrate Specificity of Lymphoid-specific Tyrosine Phosphatase (Lyp) and Identification of Src Kinase-associated Protein of 55 kDa Homolog (SKAP-HOM) as a Lyp Substrate

  Xiao Yu, Ming Chen, Sheng Zhang, Zhi-Hong Yu, Jin-Peng Sun, Lina Wang, Sijiu Liu, Tsuyoshi Imasaki, Yuichiro Takagi, Zhong-Yin Zhang

  Sep. 2011, JOURNAL OF BIOLOGICAL CHEMISTRY, 286(35) (35), 30526 - 30534, English

  [Refereed]

  Scientific journal


• Architecture of the Mediator head module

  Tsuyoshi Imasaki, Guillermo Calero, Gang Cai, Kuang-Lei Tsai, Kentaro Yamada, Francesco Cardelli, Hediye Erdjument-Bromage, Paul Tempst, Imre Berger, Guy Lorch Kornberg, Francisco J. Asturias, Roger D. Kornberg, Yuichiro Takagi

  Lead, Jul. 2011, NATURE, 475(7355) (7355), 240 - U45, English

  [Refereed]

  Scientific journal


• Crystallization and X-ray diffraction studies of DNA-free and DNA-bound forms of EcoO109I DNA methyltransferase

  Makoto Iwamoto, Asami Hishiki, Takashi Shimada, Tsuyoshi Imasaki, Junko Tsuda, Keiko Kita, Toshiyuki Shimizu, Mamoru Sato, Hiroshi Hashimoto

  Nov. 2010, ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, 66, 1528 - 1530, English

  [Refereed]

  Scientific journal


• Crystal Structure of the Human Hsmar1-Derived Transposase Domain in the DNA Repair Enzyme Metnase

  Kristie D. Goodwin, Hongzhen He, Tsuyoshi Imasaki, Suk-Hee Lee, Millie M. Georgiadis

  Jul. 2010, BIOCHEMISTRY, 49(27) (27), 5705 - 5713, English

  [Refereed]

  Scientific journal


• Mediator Head module structure and functional interactions

  Gang Cai, Tsuyoshi Imasaki, Kentaro Yamada, Francesco Cardelli, Yuichiro Takagi, Francisco J. Asturias

  Mar. 2010, NATURE STRUCTURAL & MOLECULAR BIOLOGY, 17(3) (3), 273 - U31, English

  [Refereed]

  Scientific journal


• Mediator Structural Conservation and Implications for the Regulation Mechanism

  Gang Cai, Tsuyoshi Imasaki, Yuichiro Takagi, Francisco J. Asturias

  Apr. 2009, STRUCTURE, 17(4) (4), 559 - 567, English

  [Refereed]

  Scientific journal


• Structural basis for substrate recognition and dissociation by human transportin 1

  Tsuyoshi Imasaki, Toshiyuki Shimizu, Hiroshi Hashimoto, Yuji Hidaka, Shingo Kose, Naoko Imamoto, Michiyuki Yamada, Mamoru Sato

  Oct. 2007, MOLECULAR CELL, 28(1) (1), 57 - 67, English

  [Refereed]

  Scientific journal


• Crystallization and preliminary X-ray crystallographic studies of transportin 1 in complex with nucleocytoplasmic shuttling and nuclear localization fragments

  Tsuyoshi Imasaki, Toshiyuki Shimizu, Hiroshi Hashimoto, Yuji Hidaka, Michiyuki Yamada, Mamoru Sato

  Aug. 2006, ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, 62, 785 - 787, English

  [Refereed]

  Scientific journal


• Crystal structures of type II restriction endonuclease Eco0109I and its complex with cognate DNA

  H Hashimoto, T Shimizu, T Imasaki, M Kato, N Shichijo, K Kita, M Sato

  Feb. 2005, JOURNAL OF BIOLOGICAL CHEMISTRY, 280(7) (7), 5605 - 5610, English

  [Refereed]

  Scientific journal


• Crystallization and preliminary X-ray crystallographic analyses of EcoO109I and its complex with DNA

  T Imasaki, H Hashimoto, T Shimizu, M Kato, J Tsuda, K Kita, M Sato

  Jun. 2004, ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY, 60, 1165 - 1166, English

  [Refereed]

  Scientific journal

• 最新の電子顕微鏡解析により明らかとなった心筋サルコメア構造と機能

  今崎 剛, 仁田 亮

  Jul. 2025, ファルマシア, 61(7) (7), 647 - 651, Japanese

  [Refereed][Invited]


• 骨髄微小環境ニッチによる造血幹細胞の老化制御戦略

  鈴木暖佳, 宮地洋希, 西川大生, 久野舟平, 椎名達郎, 吉川遼, 吉川知志, 今崎剛, 仁田亮, 仁田英里子

  2024, 日本解剖学会総会・全国学術集会抄録集(CD-ROM), 129th


• The molecular mechanism of non-centrosomal microtubule nucleation

  Tsuyoshi Imasaki, Ryo Nitta

  Lead, Aug. 2023, Seikagaku, Japanese

  [Refereed][Invited]


• クロマチンリモデリング因子BRMは骨髄微小環境ニッチを介して造血幹細胞を維持する

  鈴木暖佳, 宮地洋希, 西川大生, 椎名達郎, 川端野乃子, 吉川遼, 崎浜吉昭, 薛富義, 吉川知志, 今崎剛, 仁田亮, 仁田英里子

  2023, 日本解剖学会総会・全国学術集会抄録集(CD-ROM), 128th


• MAPs: microtubule associated proteins

  吉川知志, 仁田英里子, 今崎剛, 仁田亮

  (公財)金原一郎記念医学医療振興財団, Aug. 2020, 生体の科学, 71(4) (4), 298 - 303, Japanese


• Mediator Structure and Interaction with the Basal Transcription Machinery

  Francisco J. Asturias, Gang Cai, Tsuyoshi Imasaki, Kentaro Yamada, Francesco Cardelli, Yuichiro Takagi

  Apr. 2010, FASEB JOURNAL, 24, English

  Summary international conference

• イメージング時代の構造生命科学 : 細胞の動態、膜のないオルガネラ、分子の構造変化をトランススケールに観る

  田中, 啓二, 若槻, 壮市

  Contributor, 細胞骨格が制御する細胞内の営みをトランススケールに理解する (仁田亮, 今崎剛 ), 羊土社, Mar. 2020, Japanese, ISBN: 9784758103855


• 新しい臨床を開拓するための分子循環器病学

  小室, 一成

  Contributor, 分子構造解析で何が見えるか (今崎剛, 仁田英里子, 仁田亮), 南山堂, Apr. 2019, Japanese, ISBN: 9784525249410

• 細胞骨格ダイナミクスのトランススケール解析

  今崎剛

  日本薬学会第146年会, Mar. 2026

  Public symposium


• 細胞極性を決定する微小管ネットワーク形成の分子機構

  今崎剛

  第131回 日本解剖学会総会 ・ 全国学術集会, Mar. 2026

  [Invited]

  Nominated symposium


• Direct observation of CAMSAP2-induced microtubule and aster formation processes usinghigh-speed AFM and cryo-EM

  Tsuyoshi Imasaki, Ayhan Yurtsever, Ryota Kitano, Kien Xuan Ngo, Takaaki Kato, Hanjin Liu, Hideki Shigematsu, Takeshi Fukuma, Ryo Nitta

  The 63rd Annual Meeting of the Biophysical Society of Japan, Sep. 2025, English

  [Invited]

  Public symposium


• クライオ電子顕微鏡解析によるグラム陰性菌を対象とした抗菌薬の作用機構の解明

  今崎 剛

  日本顕微鏡学会 第81回学術講演会, Jun. 2025

  [Invited]

  Invited oral presentation


• Molecular mechanisms in force generation of minus-end directed kinesin 14

  Tsuyoshi Imasaki, Satoki Shibata, Hideki Shigematsu, Sharyn Endow, Ryo Nitta

  The 24th Annual Meeting of the Protein Science Society of Japan, Jun. 2024

  [Invited]

  Public symposium


• Structural basis of minus-end directed motility of dimeric kinesin-14 along microtubule

  Tsuyoshi Imasaki, Satoki Shibata, Hideki Shigematsu, Sharyn A. Endow, Ryo Nitta

  The 129th Annual Meeting of The Japanese Association of Anatomists, Mar. 2024, English

  [Invited]

  Nominated symposium


• 微小管による細胞極性形成制御機構の構造研究

  今崎 剛

  日本顕微鏡学会第 65 回シンポジウム, Nov. 2022, Japanese

  [Invited]

  Nominated symposium


• 拡張型心筋症の病態解明に向けた FIB-SEM〜クライオTEMの試み

  今崎 剛

  日本顕微鏡学会 生体解析分科会研究会 「バイオ向けクライオ透過電子顕微鏡の多様性の最前線３」, Nov. 2022, Japanese

  [Invited]


• Practical methods for in situ structural biology on clinical samples

  Tsuyoshi Imasaki

  日本顕微鏡学会 生体解析分科会研究会 on-lineミニシンポジウム「バイオ向けクライオ透過電子顕微鏡の多様性の最前線2」, Mar. 2022

  [Invited]

  Invited oral presentation


• Structural basis of microtubule dynamics inhibition by Kinesin-4

  Tsuyoshi Imasaki

  The 127th Annual Meeting of The Japanese Association of Anatomists, Mar. 2022

  Oral presentation


• Applications of in situ cryo electron microscopy in biology and medicine

  Tsuyoshi Imasaki, Satoshi Kikkawa, Hironori Inaba, Hiroko Takazaki, Takayuki Kato, Kazuhiro Aoyama, Kaoru Mitsuoka, Takao Nakata, Ryo Nitta

  The 64th Symposium of The Japanese Society of Microscopy, Nov. 2021

  Invited oral presentation


• The mechanism of microtubule nucleating center formation by CAMSAP2

  Tsuyoshi Imasaki, Satoshi Kikkawa, Saijyo Yumiko, Hideki Shigematsu, Kazuhiro Aoyama, Kaoru Mitsuoka, Masatoshi Takeichi, Ryo, Nitta

  第126回 日本解剖学会総会･全国学術集会 第98回 日本生理学会大会, Mar. 2021

  Oral presentation


• Structural mechanism of non-centrosomal microtubule nucleation

  Tsuyoshi Imasaki, Satoshi Kikkawa, Saijyo Yumiko, Hideki Shigematsu, Kazuhiro Aoyama, Kaoru Mitsuoka, Masatoshi Takeichi, Ryo, Nitta

  日本顕微鏡学会 第76回学術講演 (誌上開催), May 2020, Japanese

  [Invited]

  Nominated symposium


• Structural study of the Microtubule-MAP4 complex analyzed by Cryo-EM

  IMASAKI Tsuyoshi

  The 94th Annual Meeting of The Japanese Association of Anatomists at Kinki, Nov. 2018, Japanese, Domestic conference

  Oral presentation


• Cryo-EM analysis revealed how microtubule-associated protein 4 (MAP4) controls microtubule stability and kinesin motility

  IMASAKI Tsuyoshi

  Asia Pacific International Congress of Anatomists, Oct. 2018, English, TI_APICA8-Abstract.pdf, Others, abstract, International conference

  [Invited]

  Invited oral presentation

  添付ファイルのURL


• Integrated approach for structural biology of multisubunit complexes.

  IMASAKI Tsuyoshi

  The 39th Annal Meeting of the Molecular Biology Society of Japan, Japanese, Domestic conference

  [Invited]

  Public symposium

• 日本顕微鏡学会

  Jun. 2025 - Present


• The Japanese Association of Anatomists

  Apr. 2018 - Present


• The Molecular Biology Society of Japan

  Jul. 2010 - Present

• Mechanism of microtubule based cell polarity formation in situ

  JST, FOREST, Apr. 2022 - Mar. 2029, Principal investigator


• Molecular Mechanism Underlying Helical Growth in Plants Induced by Microtubule Biological Clusters

  今崎 剛

  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research, Grant-in-Aid for Transformative Research Areas (A), Kobe University, Apr. 2025 - Mar. 2027


• 革新的化合物探索・合成手法による新規抗菌アジュバントの創出

  鈴木 仁人, 星野 仁彦, 竹内 恒, 今崎 剛, 五十嵐 雅之, 渡辺 匠, 桑江 朝臣, 柴山 恵吾

  国立研究開発法人日本医療研究開発機構, 革新的先端研究開発支援事業, Oct. 2021 - Mar. 2027, Coinvestigator


• a

  今崎 剛

  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C), Grant-in-Aid for Scientific Research (C), Kobe University, Apr. 2022 - Mar. 2025


• Structural study of Mediator CDK module

  IMASAKI TSUYOSHI

  Japan Society for the Promotion of Science, Grants-in-Aid for Scientific Research Grant-in-Aid for Scientific Research (C), Grant-in-Aid for Scientific Research (C), Kobe University, Apr. 2019 - Mar. 2022, Principal investigator

  The transcription mediator complex is a multi-protein complex that regulates RNA polymerase II (Pol II) transcription. The transcription mediator complex is composed of four modules with more than 25 subunits, of which the CDK module, composed of four subunits, activates transcription by phosphorylation through the kinase domain and also represses through interaction with other proteins. In this study, we developed a new multi-protein complex preparation technique and analyzed the structure of the CDK module by cryo-EM single-particle analysis to elucidate one aspect of its phosphorylation function.


• Structure determination of Mediator CDK module

  IMASAKI Tsuyoshi

  JST, PRESTO, Oct. 2014 - Mar. 2018, Principal investigator

  Competitive research funding