Faculty Profiles - Kubo Tomohiro

写真a

Kubo Tomohiro

Organization

Graduate Faculty of Interdisciplinary Research Faculty of Medicine Basic Science for Clinical Medicine (Anatomy and Structural Biology) Senior Assistant Professor

Contact information

Homepage

http://www.med.yamanashi.ac.jp/basic/anat01/

Research History

Hosei University

2020.8
University of Yamanashi Senior Assistant Professor

2019.4
University of Yamanashi Medical School Department of Anatomy and Structural Biology Lecturer

2019.4
山梨大学　特任助教助教

2016.4 - 2019.3
University of Yamanashi Medical School Department of Anatomy and Structural Biology Project Assistant Professor

2016.4 - 2019.3
University of Massachusetts Medical School Cell and Developmental Biology Postdoctoral Research Associate

2014.4 - 2016.3
Postdoctoral Research Associate 　(University of Massachusetts Medical School)

2013.4 - 2016.3
University of Massachusetts Medical School Cell and Developmental Biology Postdoctoral Research Associate (Founded by Uehara Memorial Foundation)

2013.4 - 2014.3
日本学術振興会特別研究員（PD）

2012.4 - 2013.3

　 More details

Notes：2012/04/01-2013/03/31
Graduate School of Science, The University of Tokyo Department of Biological Sciences Research Fellow of the Japan Society for the Promotion of Science (PD)

2012.4 - 2013.3
日本学術振興会特別研究員(DC2)

2011.4 - 2012.3

　 More details

Notes：2011/04/01-2012-3/31
Graduate School of Science, The University of Tokyo Department of Biological Sciences Research Fellow of the Japan Society for the Promotion of Science (DC2)

2011.4 - 2012.3

▼display all

Education

The University of Tokyo

- 2012.3

　 More details

Country： Japan

Course： Doctor course
The University of Tokyo Graduate School of Science Department of Biological Sciences, Doctoral course

2009.4 - 2012.3
The University of Tokyo

- 2009.3

　 More details

Country： Japan

Course： Master course
The University of Tokyo Graduate School of Science Department of Biological Sciences, Master's course

2007.4 - 2009.3
The University of Tokyo

- 2007.3

　 More details

Country： Japan
The University of Tokyo Faculty of Science Department of Biological Sciences

2005.4 - 2007.3
The University of Tokyo Natural Sciences II

2003.4 - 2005.3

▼display all

Degree

Ph.D ( 2012.3 The University of Tokyo )

Current state of research and teaching activities

クラミドモナスという単細胞緑藻類を用いて、真核生物の鞭毛（繊毛と同義）の構築機構と運動機構を研究している。

Research Areas

Life Science / Cell biology
Life Science / Cell biology
Life Science / Biophysics

Research Interests

Cilia/flagella, Axonemal dynein, Chlamydomonas reinhardtii, Posttranslational modification, Tubulin polyglutamylation, Intraflagellar transport
Chlamydomonas
Flagellum
Post-translational modification
Cilium
Polyglutamylation
Tubulin
Dynein

Subject of research

Studies on the regulation of flagellar/ciliary motility by tubulin polyglutamylation

Research Projects

真核生物の鞭毛で新規に見つかった蛋白質合成系の解明

2023.4 - 2026.3

基盤研究C

久保智広

　 More details

Authorship：Principal investigator Type of fund：：Science research expense
真核生物の鞭毛で新規に見つかった蛋白質合成系の解明

Grant number：23K05829 2023.4 - 2026.3

日本学術振興会科学研究費助成事業基盤研究(C) 基盤研究(C)

久保智広
真核生物の鞭毛に局在する蛋白質合成系の機能解明

2023.4 - 2025.3

久保智広

　 More details

Authorship：Principal investigator Type of fund：：Science research expense
微細藻類の鞭毛に存在する蛋白質合成系の解明

2023.4 - 2025.3

久保智広

　 More details

Authorship：Principal investigator Type of fund：：Science research expense
微細藻類の鞭⽑に存在する蛋⽩質合成系の解明

2023.4 - 2025.3

公益財団法人発酵研究所一般研究助成

久保智広

　 More details

Authorship：Principal investigator Grant type：Competitive
真核生物の鞭毛に局在する蛋白質合成系の機能解明

2023.4 - 2025.3

公益財団法人加藤記念バイオサイエンス振興財団研究助成「バイオテクノロジー分野」

久保智広

　 More details

Authorship：Principal investigator Grant type：Competitive
鞭毛繊毛の構築に必須なチューブリン供給システムの解明

2022.4 - 2023.3

公益財団法人小柳財団研究助成金

久保智広
鞭毛繊毛の構築に必須なチューブリン供給システムの解明

2022.4 - 2023.3

公益財団法人小柳財団研究助成金

久保智広

　 More details

Authorship：Principal investigator Grant type：Competitive
鞭毛構築に必須な鞭毛前駆体の実体解明

2021.4 - 2022.3

上原記念生命科学財団　研究奨励金

久保智広

　 More details

Authorship：Principal investigator Type of fund：：Science research expense
鞭毛構築に必須な鞭毛前駆体の実体解明

2021.4 - 2022.3

公益財団法人上原記念生命科学財団研究奨励金

久保智広

　 More details

Authorship：Principal investigator
カルシウムイオン依存的な鞭毛構築機構の解明

Grant number：19K16123 2019.4 - 2022.3

Japan Society for the Promotion of Science University of Yamanashi Grants-in-Aid for Scientific Research Grant-in-Aid for Early-Career Scientists Grant-in-Aid for Early-Career Scientists

Kubo Tomohiro

　 More details

Calcium ion is involved in various biological functions such as muscle contraction, neurotransmission, gene expression, and waveform conversion of cilia/flagella. Calcium ion is known to be important for the assembly of cilia/flagella, but precise molecular mechanism is unclear. In this study, I used a unicellular green alga, Chlamydomonas reinhardtii, to investigate calcium ion dependent flagellar assembly. I found that depolymerization kinesin may be controlled by calcium ion during flagellar regeneration of Chlamydomonas.
カルシウムイオン依存的な鞭毛構築機構の解明

2019.4 - 2021.3

若手研究

久保智広

　 More details

Authorship：Principal investigator Type of fund：：Science research expense
チューブリンポリグルタミン酸化修飾による鞭毛構築機構の解明

2017.11

公益財団法人　武田科学振興財団

久保智広
チューブリンポリグルタミン酸化修飾による鞭毛構築機構の解明

2017.11

公益財団法人武田科学振興財団

久保智広

　 More details

Authorship：Principal investigator Grant type：Competitive
チューブリンポリグルタミン酸化修飾による鞭毛繊毛構築メカニズムの解明

2017.4 - 2019.3

若手研究B

久保智広

　 More details

Authorship：Principal investigator Type of fund：：Science research expense
Elucidation of flagellar/ciliary assembly mechanism by tubulin polyglutamylation

2017.4 - 2019.3

Japan Society for the Promotion of Science Grant-in-Aid for Young Scientists (B)

Tomohiro Kubo

　 More details

Authorship：Principal investigator Grant type：Competitive
チューブリンポリグルタミン酸化修飾による鞭毛・繊毛運動機構の追究

2016.10 - 2017.10

公益財団法人金原一郎記念医学医療振興財団基礎医学医療研究助成金報告書基礎医学医療研究

久保智広

　 More details

Authorship：Principal investigator Type of fund：：Others
チューブリンポリグルタミン酸化修飾による鞭毛・繊毛運動機構の追究

2016.10 - 2017.10

公益財団法人金原一郎記念医学医療振興財団

久保智広

　 More details

Authorship：Principal investigator Grant type：Competitive
チューブリン・ポリグルタミン酸化修飾による鞭毛運動調節機構の解明

Grant number：11J08873 2011 - 2012

日本学術振興会科学研究費助成事業特別研究員奨励費

久保智広

　 More details

具体的内容
当該研究の目的は、鞭毛におけるチューブリン・ポリグルタミン酸化修飾の重要性を追求することである。この目的を達成するために、具体的に二つの実験テーマを設定した。そのひとつはチューブリン・ポリグルタミン酸化修飾が鞭毛運動性に対してどのような影響を及ぼすのかを明らかにすることである。本研究では、この目的を達成するために、鞭毛のポリグルタミン酸化修飾が減少したクラミドモナス変異株tpg1を用いて解析を行った。その結果、ポリグルタミン酸化修飾は複数種類ある軸糸ダイニンのうち、特定の一種の内腕ダイニンに対して大きな影響を持つことが明らかになった。さらに、本研究の二つ目の実験テーマは、ポリグルタミン酸化修飾を行う修飾酵素がどのように鞭毛内へと輸送されるのかを明らかにすることである。本研究ではtpg1と類似な表現型を示すクラミドモナス変異株tpg2の解析によって、修飾酵素TTLL9と複合体を形成する新規の鞭毛蛋白質FAP234を同定した。TTLL9-FAP234複合体は鞭毛内輸送系によって鞭毛内へと運ばれることが明らかになった。これらの成果を、アメリカ細胞生物学会を含む国内外の学会で発表し好評を得た。
意義・重要性
チューブリン・ポリグルタミン酸化修飾は鞭毛運動においてダイニンの運動性に影響を及ぼすことが先行研究によって予想されていたが、ダイニンに対して具体的にどのような影響を与えるかは全く分かっていなかった。本研究ではポリグルタミン酸化修飾が特定の内腕ダイニンー種とおそらく強い静電相互作用することを初めて明らかにした。このことはダイニンと微小管の相互作用を理解するうえで重要な結果である。

▼display all

Papers

Tubulin glycylation controls ciliary motility through modulation of outer-arm dyneins Reviewed Major achievement

Tomohiro Kubo, Rinka Sasaki, Toshiyuki Oda

Molecular Biology of the Cell 2024.5( ISSN：1059-1524 eISSN：1939-4586 )

　More details

Language：English Publishing type：Research paper (scientific journal) Publisher：American Society for Cell Biology (ASCB)

Tubulins undergo several post-translational modifications (PTMs) including glutamylation and glycylation. The contribution of these PTMs to the motilities of cilia and flagella is still unclear. Here, we investigated the role of tubulin glycylation by examining a novel Chlamydomonas mutant lacking TTLL3, an enzyme responsible for initiating glycylation. Immunostaining of cells and flagella revealed that glycylation is only restricted to the axonemal tubulin composing the outer-doublet but not the central-pair microtubules. Furthermore, the flagellar localization of TTLL3 was found to be dependent on intraflagellar transport. The mutant, ttll3(ex5), completely lacks glycylation and consequently exhibits slower swimming velocity compared to the wild-type strain. By combining the ttll3(ex5) mutation with multiple axonemal dynein deficient mutants, we found that the lack of glycylation does not affect the motility of the outer-arm dynein lacking mutations. Sliding disintegration assay using isolated axonemes revealed that the lack of glycylation decreases microtubule sliding velocity in the normal axoneme but not in the axoneme lacking the outer-arm dyneins. Based on our recent study that glycylation occurs exclusively on β-tubulin in Chlamydomonas, these findings suggest that tubulin glycylation controls flagellar motility through modulating outer-arm dyneins, presumably by neutralizing the negative charges of glutamate residues at the C-terminus region of β-tubulin. (200 words)

DOI： 10.1091/mbc.e24-04-0154

DOI： 10.1091/mbc.e24-04-0154
α- and β-tubulin C-terminal tails with distinct modifications are crucial for ciliary motility and assembly Reviewed Major achievement

Tomohiro Kubo, Yuma Tani , Haru-Aki Yanagisawa, Masahide Kikkawa, Toshiyuki Oda

Journal of Cell Science 2023.7( ISSN：0021-9533 eISSN：1477-9137 )

　More details

Authorship：Lead author,　Corresponding author Language：English Publishing type：Research paper (scientific journal) Publisher：The Company of Biologists

α- and β-tubulin have an unstructured glutamate-rich region at their C-terminal tails (CTT). The function of this region in cilia/flagella is still unclear, except that glutamates in CTT act as the sites for posttranslational modifications that affect ciliary motility. A unicellular alga Chlamydomonas possesses only two a-tubulin genes and two b-tubulin genes, each pair encoding an identical protein. This simple gene organization may enable a complete replacement of the wild-type tubulin with its mutated version. Here, using CRISPR/Cas9, we generated mutants expressing tubulins with modified CTTs. We found that the mutant whose four glutamate residues in the α-tubulin CTT have been replaced by alanine almost completely lacked polyglutamylated tubulin and displayed paralyzed cilia. In contrast, the mutant lacking the glutamate-rich region of the β-tubulin CTT assembled short cilia without the central apparatus. This phenotype is similar to the mutants harboring a mutation in a subunit of katanin, whose function has been shown to depend on the b-tubulin CTT. Therefore, our study reveals distinct and important roles of α- and β-tubulin CTT in the formation and function of cilia.

DOI： 10.1242/jcs.261070
Chlamydomonas FAP70 is a component of the previously uncharacterized ciliary central apparatus projection C2a Reviewed Major achievement

Yuqing Hou, Lei Zhao, Tomohiro Kubo, Xi Cheng, Nathan McNeill, Toshiyuki Oda, George B. Witman

JOURNAL OF CELL SCIENCE 2021.5( ISSN：0021-9533 )

　More details

Language：English Publishing type：Research paper (scientific journal)
Chlamydomonas FAP70 is a component of the previously uncharacterized ciliary central apparatus projection C2a Reviewed Major achievement

Yuqing Hou, Lei Zhao, Tomohiro Kubo, Xi Cheng, Nathan McNeill, Toshiyuki Oda, George B. Witman

Journal of Cell Science 2021.5( ISSN：0021-9533 eISSN：1477-9137 )

　More details

Language：English Publishing type：Research paper (scientific journal) Publisher：The Company of Biologists

Cilia are essential organelles required for cell signaling and motility. Nearly all motile cilia have a “9+2” axoneme composed of 9 outer doublet microtubules plus 2 central microtubules; the central microtubules together with their projections is termed the central apparatus (CA). In Chlamydomonas reinhardtii, a model organism for studying cilia, 30 proteins are known CA components, and ∼36 more are predicted to be CA proteins. Among the candidate CA proteins is the highly conserved FAP70, which also has been reported to be associated with the doublet microtubules. Here we determined by super-resolution structured illumination microscopy that FAP70 is located exclusively in the CA, and show by cryo-electron microscopy that its N-terminus is located at the base of the CA's C2a projection. We also found that fap70-1 mutant axonemes lack most of the C2a projection. Mass spectrometry revealed that fap70-1 axonemes lack not only FAP70 but two other conserved candidate CA proteins, FAP65 and FAP147. Finally, FAP65 and FAP147 co-immunoprecipitated with HA-tagged FAP70. Taken together, these data identify FAP70, FAP65, and FAP147 as the first defining components of the C2a projection.

DOI： 10.1242/jcs.258540

PubMed
Diffusion rather than IFT likely provides most of the tubulin required for axonemal assembly Reviewed Major achievement

Julie Craft Van De Weghe, J. Aaron Harris, Tomohiro Kubo, George B. Witman, Karl F. Lechtreck

JOURNAL OF CELL SCIENCE jcs.249805 - jcs.249805 2020.8( ISSN：0021-9533 eISSN：1477-9137 )

　More details

Language：English Publishing type：Research paper (scientific journal) Publisher：The Company of Biologists (United Kingdom)

Tubulin enters the cilium by diffusion and motor-based intraflagellar transport (IFT). However, the respective contribution of each route in providing tubulin for axonemal assembly remains unknown. Using <italic>Chlamydomonas</italic>, we attenuated IFT-based tubulin transport of GFP-β-tubulins by altering the IFT74/IFT81 tubulin-binding module and the C-terminal E-hook of tubulin. E-hook deficient GFP-β-tubulin is incorporated into the axonemal microtubules, but its transport frequency by IFT was reduced by ∼90% in control cells and essentially abolished when the IFT81 tubulin-binding site was incapacitated. Despite the strong reduction in IFT, the proportion of E-hook deficient GFP-β-tubulin in the axoneme was only moderately reduced. In vivo imaging showed more GFP-β-tubulin particles entering cilia by diffusion than by IFT. Extrapolated to endogenous tubulin, the data indicate that diffusion provides most of the tubulin required for axonemal assembly. We propose that IFT of tubulin is nevertheless needed for ciliogenesis because it augments the tubulin pool supplied to the ciliary tip by diffusion, thus ensuring that free tubulin there is maintained at the critical concentration for plus-end microtubule assembly during rapid ciliary growth.

DOI： 10.1242/jcs.249805
TIM, a targeted insertional mutagenesis method utilizing CRISPR/Cas9 in Chlamydomonas reinhardtii Reviewed Major achievement

Picariello T, Hou Y, Kubo T, McNeill NA, Yanagisawa HA, Oda T, Witman GB

PLoS One 15 ( 5 ) e0232594 - e0232594 2020.5( ISSN：1932-6203 eISSN：1932-6203 )

　More details

Language：English Publishing type：Research paper (scientific journal) Publisher：Public Library of Science (PLOS)

DOI： 10.1371/journal.pone.0232594
Regulation of eukaryotic flagellar motility by tubulin polyglutamylation Invited Major achievement

Tomohiro Kubo

51 ( 12 ) 37 - 42 2019.10

　More details

Authorship：Lead author,　Last author,　Corresponding author Language：Japanese
Chlamydomonas as a tool to study tubulin polyglutamylation. Invited Reviewed Major achievement

Kubo T and Oda T.

Microscopy 2018.10( ISSN：2050-5698 )

　More details

Authorship：Lead author,　Corresponding author Language：English Publishing type：(MISC) Introduction and explanation (scientific journal)
Chlamydomonas as a tool to study tubulin polyglutamylation. Invited Reviewed Major achievement

Microscopy 2018.10

　More details

Authorship：Lead author,　Corresponding author Language：English Publishing type：Research paper (scientific journal)
CFAP70 is a Novel Axoneme-Binding Protein that Localizes at the Base of the Outer Dynein Arm and Regulates Ciliary Motility. Reviewed Major achievement

Shamoto N, Narita K, Kubo T, Oda T, and Takeda S.

Cells 2018.8( ISSN：2073-4409 )

　More details

Language：English Publishing type：Research paper (scientific journal)
CFAP70 Is a Novel Axoneme-Binding Protein That Localizes at the Base of the Outer Dynein Arm and Regulates Ciliary Motility. Reviewed Major achievement

Noritoshi Shamoto, Keishi Narita, Tomohiro Kubo, Toshiyuki Oda, Sen Takeda

Cells 7 ( 9 ) 2018.8

　More details

Language：English Publishing type：Research paper (scientific journal)
A microtubule-dynein tethering complex regulates the axonemal inner dynein f (I1) Reviewed

Tomohiro Kubo, Yuqing Hou, Deborah A. Cochran, George B. Witman, Toshiyuki Oda

Molecular Biology of the Cell 29 ( 9 ) 1060 - 1074 2018.5( ISSN：1939-4586 )

　More details

Authorship：Lead author Language：English Publishing type：Research paper (scientific journal) Publisher：American Society for Cell Biology

Motility of cilia/flagella is generated by a coordinated activity of thousands of dyneins. Inner dynein arms (IDAs) are particularly important for the formation of ciliary/flagellar waveforms, but the molecular mechanism of IDA regulation is poorly understood. Here we show using cryoelectron tomography and biochemical analyses of Chlamydomonas flagella that a conserved protein FAP44 forms a complex that tethers IDA f (I1 dynein) head domains to the A-tubule of the axonemal outer doublet microtubule. In wild-type flagella, IDA f showed little nucleotide-dependent movement except for a tilt in the fβ head perpendicular to the microtubule-sliding direction. In the absence of the tether complex, however, addition of ATP and vanadate caused a large conformational change in the IDA f head domains, suggesting that the movement of IDA f is mechanically restricted by the tether complex. Motility defects in flagella missing the tether demonstrates the importance of the IDA f-tether interaction in the regulation of ciliary/flagellar beating.

DOI： 10.1091/mbc.E17-11-0689

Scopus
A microtubule-dynein tethering complex regulates the axonemal inner dynein f (I1). Reviewed Major achievement

MOLECULAR BIOLOGY OF THE CELL 2018.3( ISSN：1059-1524 )

　More details

Authorship：Lead author Language：English Publishing type：Research paper (scientific journal) Publisher：The American Society for Cell Biology
Electrostatic interaction between polyglutamylated tubulin and the nexin-dynein regulatory complex regulates flagellar motility Reviewed Major achievement

Tomohiro Kubo, Toshiyuki Oda

MOLECULAR BIOLOGY OF THE CELL 28 ( 17 ) 2260 - 2266 2017.8( ISSN：1059-1524 eISSN：1939-4586 )

　More details

Authorship：Lead author Language：English Publishing type：Research paper (scientific journal) Publisher：AMER SOC CELL BIOLOGY

Tubulins undergo various posttranslational modifications. Among them, polyglutamylation is involved in the motility of eukaryotic flagella and the stability of the axonemal microtubules. However, it remains unclear where polyglutamylated tubulin localizes precisely within the axoneme and how tubulin polyglutamylation affects flagellar motility. In this study, we identified the three-dimensional localization of the polyglutamylated tubulin in Chlamydomonas flagella using antibody labeling and cryo-electron tomography. Polyglutamylated tubulins specifically located in close proximity to a microtubule-cross-bridging structure called the nexin-dynein regulatory complex (N-DRC). Because N-DRC is positively charged, we hypothesized that there is an electrostatic interaction between the polyglutamylated tubulin and the N-DRC, and therefore we mutated the amino acid sequences of DRC4 to modify the charge of the N-DRC. We found that both augmentation and reduction of the positive charge on DRC4 resulted in reduced flagellar motility. Moreover, reduced motility in a mutant with a structurally defective N-DRC was partially restored by increasing the positive charge on DRC4. These results clearly indicate that beating motion of flagella is maintained by the electrostatic cross-bridge formed between the negatively charged polyglutamylated tubulins and the positively charged N-DRC.

DOI： 10.1091/mbc.E17-05-0285

Web of Science
Electrostatic interaction between polyglutamylated tubulin and the nexin-dynein regulatory complex regulates flagellar motility. Reviewed Major achievement

Tomohiro Kubo and Toshiyuki Oda

MOLECULAR BIOLOGY OF THE CELL 2017.6( ISSN：1059-1524 )

　More details

Authorship：Lead author Language：English Publisher：The American Society for Cell Biology
RABL2 interacts with the intraflagellar transport-B complex and CEP19 and participates in ciliary assembly. Reviewed Major achievement

Yuya Nishijima, Yohei Hagiya, Tomohiro Kubo, Ryota Takei, Yohei Katoh, and Kazuhisa Nakayama

MOLECULAR BIOLOGY OF THE CELL 28 ( 12 ) 1652 - 1666 2017.6( ISSN：1059-1524 )

　More details

Language：English Publisher：The American Society for Cell Biology
RABL2 interacts with the intraflagellar transport-B complex and CEP19 and participates in ciliary assembly Reviewed Major achievement

Yuya Nishijima, Yohei Hagiya, Tomohiro Kubo, Ryota Takei, Yohei Katoh, Kazuhisa Nakayama

MOLECULAR BIOLOGY OF THE CELL 28 ( 12 ) 1652 - 1666 2017.6( ISSN：1059-1524 eISSN：1939-4586 )

　More details

Language：English Publishing type：Research paper (scientific journal) Publisher：AMER SOC CELL BIOLOGY

Proteins localized to the basal body and the centrosome play crucial roles in ciliary assembly and function. Although RABL2 and CEP19 are conserved in ciliated organisms and have been implicated in ciliary/flagellar functions, their roles are poorly understood. Here we show that RABL2 interacts with CEP19 and is recruited to the mother centriole and basal body in a CEP19-dependent manner and that CEP19 is recruited to the centriole probably via its binding to the centrosomal protein FGFR1OP. Disruption of the RABL2 gene in Chlamydomonas reinhardtii results in the nonflagellated phenotype, suggesting a crucial role of RABL2 in ciliary/flagellar assembly. We also show that RABL2 interacts, in its GTP-bound state, with the intraflagellar transport (IFT)-B complex via the IFT74-IFT81 heterodimer and that the interaction is disrupted by a mutation found in male infertile mice (Mot mice) with a sperm flagella motility defect. Intriguingly, RABL2 binds to CEP19 and the IFT74-IFT81 heterodimer in a mutually exclusive manner. Furthermore, exogenous expression of the GDPlocked or Mot-type RABL2 mutant in human cells results in mild defects in ciliary assembly. These results indicate that RABL2 localized to the basal body plays crucial roles in ciliary/flagellar assembly via its interaction with the IFT-B complex.

DOI： 10.1091/mbc.E17-01-0017

Web of Science
Together, the IFT81 and IFT74 N-termini form the main module for intraflagellar transport of tubulin. Reviewed Major achievement

JOURNAL OF CELL SCIENCE 129 ( 10 ) 2106 - 2119 2016.5( ISSN：0021-9533 )

　More details

Authorship：Lead author Language：English
Together, the IFT81 and IFT74 N-termini form the main module for intraflagellar transport of tubulin Reviewed Major achievement

Tomohiro Kubo, Jason M. Brown, Karl Bellve, Branch Craige, Julie M. Craft, Kevin Fogarty, Karl F. Lechtreck, George B. Witman

JOURNAL OF CELL SCIENCE 129 ( 10 ) 2106 - 2119 2016.5( ISSN：0021-9533 eISSN：1477-9137 )

　More details

Authorship：Lead author Language：English Publishing type：Research paper (scientific journal) Publisher：COMPANY OF BIOLOGISTS LTD

The assembly and maintenance of most cilia and flagella rely on intraflagellar transport (IFT). Recent in vitro studies have suggested that, together, the calponin-homology domain within the IFT81 N-terminus and the highly basic N-terminus of IFT74 form a module for IFT of tubulin. By using Chlamydomonas mutants for IFT81 and IFT74, we tested this hypothesis in vivo. Modification of the predicted tubulin-binding residues in IFT81 did not significantly affect basic anterograde IFT and length of steady-state flagella but slowed down flagellar regeneration, a phenotype similar to that seen in a strain that lacks the IFT74 N-terminus. In both mutants, the frequency of tubulin transport by IFT was greatly reduced. A double mutant that combined the modifications to IFT81 and IFT74 was able to form only very short flagella. These results indicate that, together, the IFT81 and IFT74 N-termini are crucial for flagellar assembly, and are likely to function as the main module for IFT of tubulin.

DOI： 10.1242/jcs.187120

Web of Science
Reduced tubulin polyglutamylation suppresses flagellar shortness in Chlamydomonas. Reviewed Major achievement

MOLECULAR BIOLOGY OF THE CELL 26 ( 15 ) 2810 - 2822 2015.8( ISSN：1059-1524 )

　More details

Authorship：Lead author Language：English
Reduced tubulin polyglutamylation suppresses flagellar shortness in Chlamydomonas Reviewed Major achievement

Tomohiro Kubo, Masafumi Hirono, Takumi Aikawa, Ritsu Kamiya, George B. Witman

MOLECULAR BIOLOGY OF THE CELL 26 ( 15 ) 2810 - 2822 2015.8( ISSN：1059-1524 eISSN：1939-4586 )

　More details

Authorship：Lead author Language：English Publishing type：Research paper (scientific journal) Publisher：AMER SOC CELL BIOLOGY

Ciliary length control is an incompletely understood process essential for normal ciliary function. The flagella of Chlamydomonas mutants lacking multiple axonemal dyneins are shorter than normal; previously it was shown that this shortness can be suppressed by the mutation suppressor of shortness 1 (ssh1) via an unknown mechanism. To elucidate this mechanism, we carried out genetic analysis of ssh1 and found that it is a new allele of TPG2 (hereafter tpg2-3), which encodes FAP234 functioning in tubulin polyglutamylation in the axoneme. Similar to the polyglutamylation-deficient mutants tpg1 and tpg2-1, tpg2-3 axonemal tubulin has a greatly reduced level of long polyglutamate side chains. We found that tpg1 and tpg2-1 mutations also promote flagellar elongation in short-flagella mutants, consistent with a polyglutamylation-dependent mechanism of suppression. Double mutants of tpg1 or tpg2-1 and fla10-1, a temperature-sensitive mutant of intraflagellar transport, underwent slower flagellar shortening than fla10-1 at restrictive temperatures, indicating that the rate of tubulin disassembly is decreased in the polyglutamylation-deficient flagella. Moreover, alpha-tubulin incorporation into the flagellar tips in temporary dikaryons was retarded in polyglutamylation-deficient flagella. These results show that polyglutamylation deficiency stabilizes axonemal microtubules, decelerating axonemal disassembly at the flagellar tip and shifting the axonemal assembly/disassembly balance toward assembly.

DOI： 10.1091/mbc.E15-03-0182

Web of Science
Assembly of IFT Trains at the Ciliary Base Depends on IFT74. Reviewed

CURRENT BIOLOGY 25 1583 - 1593 2015.6( ISSN：0960-9822 )

　More details

Language：English
Assembly of IFT Trains at the Ciliary Base Depends on IFT74 Reviewed Major achievement

Jason M. Brown, Deborah A. Cochran, Branch Craige, Tomohiro Kubo, George B. Witman

CURRENT BIOLOGY 25 ( 12 ) 1583 - 1593 2015.6( ISSN：0960-9822 eISSN：1879-0445 )

　More details

Language：English Publishing type：Research paper (scientific journal) Publisher：CELL PRESS

Intraflagellar transport (IFT) moves IFT trains carrying cargoes from the cell body into the flagellum and from the flagellum back to the cell body. IFT trains are composed of complexes IFT-A and IFT-B and cargo adaptors such as the BBSome. The IFT-B core proteins IFT74 and IFT81 interact directly through central and C-terminal coiled-coil domains, and recently it was shown that the N termini of these proteins form a tubulin-binding module important for ciliogenesis. To investigate the function of IFT74 and its domains in vivo, we have utilized Chlamydomonas reinhardtii ift74 mutants. In a null mutant, lack of IFT74 destabilized IFT-B, leading to flagella assembly failure. In this null background, expression of IFT74 lacking 130 amino acids (aa) of the charged N terminus stabilized IFT-B and promoted slow assembly of nearly full-length flagella. A further truncation (lacking aa 1-196, including part of coiled-coil 1) also stabilized IFT-B, but failure in IFT-A/IFT-B interaction within the pool at the base of the flagellum prevented entry of IFT-A into the flagellum and led to severely decreased IFT injection frequency and flagellar-assembly defects. Decreased IFT-A in these short flagella resulted in aggregates of stalled IFT-B in the flagella. We conclude that IFT74 is required to stabilize IFT-B; aa 197-641 are sufficient for this function in vivo. The N terminus of IFT74 may be involved in, but is not required for, tubulin entry into flagella. It is required for association of IFT-A and IFT-B at the base of the flagellum and flagellar import of IFT-A.

DOI： 10.1016/j.cub.2015.04.060

Web of Science
A conserved flagella-associated protein in Chlamydomonas, FAP234, is essential for axonemal localization of tubulin polyglutamylase TTLL9. Reviewed Major achievement

MOLECULAR BIOLOGY OF THE CELL 25 107 - 117 2014.1( ISSN：1059-1524 )

　More details

Authorship：Lead author Language：English
A conserved flagella-associated protein in Chlamydomonas, FAP234, is essential for axonemal localization of tubulin polyglutamylase TTLL9 Reviewed

Tomohiro Kubo, Haru-aki Yanagisawa, Zhongmei Liu, Rie Shibuya, Masafumi Hirono, Ritsu Kamiya

MOLECULAR BIOLOGY OF THE CELL 25 ( 1 ) 107 - 117 2014.1( ISSN：1059-1524 eISSN：1939-4586 )

　More details

Authorship：Lead author Language：English Publishing type：Research paper (scientific journal) Publisher：AMER SOC CELL BIOLOGY

Tubulin undergoes various posttranslational modifications, including polyglutamylation, which is catalyzed by enzymes belonging to the tubulin tyrosine ligase-like protein (TTLL) family. A previously isolated Chlamydomonas reinhardtii mutant, tpg1, carries a mutation in a gene encoding a homologue of mammalian TTLL9 and displays lowered motility because of decreased polyglutamylation of axonemal tubulin. Here we identify a novel tpg1-like mutant, tpg2, which carries a mutation in the gene encoding FAP234, a flagella-associated protein of unknown function. Immunoprecipitation and sucrose density gradient centrifugation experiments show that FAP234 and TTLL9 form a complex. The mutant tpg1 retains FAP234 in the cell body and flagellar matrix but lacks it in the axoneme. In contrast, tpg2 lacks both TTLL9 and FAP234 in all fractions. In fla10, a temperature-sensitive mutant deficient in intraflagellar transport (IFT), both TTLL9 and FAP234 are lost from the flagellum at nonpermissive temperatures. These and other results suggest that FAP234 functions in stabilization and IFT-dependent transport of TTLL9. Both TTLL9 and FAP234 are conserved in most ciliated organisms. We propose that they constitute a polyglutamylation complex specialized for regulation of ciliary motility.

DOI： 10.1091/mbc.E13-07-0424

Web of Science
A suppressor mutant, ssh1, of flagellar shortness in dynein-deficient Chlamydomonas strains is deficient in the gene encoding FAP234, a protein involved in tubulin polyglutamylation Major achievement

T. Kubo, M. Hirono, T. Aikawa, G. B. Witman, R. Kamiya

MOLECULAR BIOLOGY OF THE CELL 24 2013( ISSN：1059-1524 eISSN：1939-4586 )

　More details

Authorship：Lead author Language：English Publishing type：(MISC) Summary of the papers read (international conference) Publisher：AMER SOC CELL BIOLOGY

Web of Science
Tubulin polyglutamylation regulates flagellar motility by controlling a specific inner-arm dynein that interacts with the dynein regulatory complex. Reviewed Major achievement

Cytoskeleton 69 ( 12 ) 1059 - 1068 2012.12( ISSN：1949-3584 )

　More details

Authorship：Lead author Language：English
Tubulin Polyglutamylation Regulates Flagellar Motility by Controlling a Specific Inner-Arm Dynein that Interacts With the Dynein Regulatory Complex Reviewed Major achievement

Tomohiro Kubo, Toshiki Yagi, Ritsu Kamiya

CYTOSKELETON 69 ( 12 ) 1059 - 1068 2012.12( ISSN：1949-3584 )

　More details

Authorship：Lead author Language：English Publishing type：Research paper (scientific journal) Publisher：WILEY-BLACKWELL

The tpg1 mutant of Chlamydomonas lacks the tubulin polyglutamylase TTLL9 and is deficient in flagellar tubulin polyglutamylation. It exhibits slow swimming, whereas the double mutant with oda2 (a slow-swimming mutant that lacks outer-arm dynein) is completely nonmotile. Thus, tubulin polyglutamylation must be important for the functioning of inner-arm dynein(s). In this study, we show that the tpg1 mutation only slightly affects the motility of mutants that lack dynein "e," one of the seven species of major inner-arm dyneins, whereas it greatly reduces the motility of mutants lacking other inner-arm dynein species. This suggests that dynein e is the main target of motility regulation by tubulin polyglutamylation. Furthermore, the motility of various mutants in the background of the tpg1 mutation raises the possibility that tubulin polyglutamylation also affects the dynein regulatory complex, a dynein e-associated key regulator of flagellar motility, which possibly constitutes the interdoublet (nexin) link. Tubulin polyglutamylation thus may play a central role in the regulation of ciliary and flagellar motility. (C) 2012 Wiley Periodicals, Inc

DOI： 10.1002/cm.21075

Web of Science
3PS003 Tubulin polyglutamylation regulates axonemal motility by modulating the function of a specific inner-arm dynein species(The 50th Annual Meeting of the Biophysical Society of Japan)

Kubo Tomohiro, Yagi Toshiki, Kamiya Ritsu

Seibutsu Butsuri 52 S146 2012

　More details

Authorship：Lead author Language：English Publisher：The Biophysical Society of Japan General Incorporated Association

DOI： 10.2142/biophys.52.S146_3
A novel Chlamydomonas mutant, tpg2, reveals a conserved 177-kDa protein crucial for the localization of TTLL9, an enzyme that catalyzes tubulin polyglutamylation in the axoneme. Major achievement

T. Kubo, H-A. Yanagisawa, Z. Liu, R. Shibuya, M. Hirono, R. Kamiya

MOLECULAR BIOLOGY OF THE CELL 23 2012( ISSN：1059-1524 eISSN：1939-4586 )

　More details

Authorship：Lead author Language：English Publishing type：(MISC) Summary of the papers read (international conference) Publisher：AMER SOC CELL BIOLOGY

Web of Science
1K1536 Tubulin Polyglutamylation Regulates Flagellar Motility Through the Function of Dynein Regulatory Complex(Cell biology 1,The 49th Annual Meeting of the Biophysical Society of Japan) Major achievement

Kubo Tomohiro, Kamiya Ritsu

Seibutsu Butsuri 51 S58 - S59 2011

　More details

Authorship：Lead author Language：English Publisher：The Biophysical Society of Japan General Incorporated Association

DOI： 10.2142/biophys.51.S58_6
Tubulin polyglutamylation regulates axonemal motility by modulating activities on inner-arm dyneins. Reviewed Major achievement

Current Biology 20 ( 5 ) 441 - 445 2010.3( ISSN：0960-9822 )

　More details

Authorship：Lead author Language：English
Tubulin Polyglutamylation Regulates Axonemal Motility by Modulating Activities of Inner-Arm Dyneins Reviewed Major achievement

Tomohiro Kubo, Haru-aki Yanagisawa, Toshiki Yagi, Masafumi Hirono, Ritsu Kamiya

CURRENT BIOLOGY 20 ( 5 ) 441 - 445 2010.3( ISSN：0960-9822 )

　More details

Authorship：Lead author Language：English Publishing type：Research paper (scientific journal) Publisher：CELL PRESS

Tubulin polyglutamylation is a modification that adds multiple glutamates to the gamma-carboxyl group of a glutamate residue in the C-terminal tails of alpha- and beta-tubulin [1, 2]. This modification has been implicated in the regulation of axonal transport and ciliary motility. However, its molecular function in cilia remains unknown. Here, using a novel Chlamydomonas reinhardtii mutant (tpg1) that lacks a homolog of human TTLL9, a glutamic acid ligase enzyme [3], we found that the lack of a long polyglutamate side chain in alpha-tubulin moderately weakens flagellar motility without noticeably impairing the axonemal structure. Furthermore, the double mutant of tpg1 with oda2, a mutation that leads to loss of outer-arm dynein, completely lacks motility. More surprisingly, when treated with protease and ATIP, the axoneme of this paralyzed double mutant displayed faster microtubule sliding than the motile oda2 axoneme. These and other results suggest that polyglutamylation directly regulates microtubule-dynein interaction mainly by modulating the function of inner-arm dyneins.

DOI： 10.1016/j.cub.2009.12.058

Web of Science
3P166 Tubulin Polyglutamylation Regulates Flagellar Motility by Affecting Functions of Inner-Arm Dyneins(Molecular motor,The 48th Annual Meeting of the Biophysical Society of Japan)

Kubo Tomohiro, Yanagisawa Haru-aki, Yagi Toshiki, Hirono Masafumi, Kamiya Ritsu

Seibutsu Butsuri 50 ( 2 ) S174 2010

　More details

Authorship：Lead author Language：English Publisher：The Biophysical Society of Japan General Incorporated Association

DOI： 10.2142/biophys.50.S174_2

▼display all

Books and Other Publications

Regulation of eukaryotic flagellar motility by tubulin polyglutamylation

Tomohiro Kubo（ Role： Joint Work）

2020.3

　More details

Language：Japanese
Regulation of eukaryotic flagellar motility by tubulin polyglutamylation

（ Role： Joint Work）

2020.1

　More details

Responsible for pages：63-69 Language：Japanese
Regulation of eukaryotic flagellar motility by tubulin polyglutamylation Major achievement

Tomohiro Kubo（ Role： Joint Work）

2019.11

　More details

Language：Japanese
Regulation of eukaryotic flagellar motility by tubulin polyglutamylation Major achievement

Tomohiro Kubo（ Role： Joint Work）

2019.10

　More details

Language：Japanese

Presentations

Tubulin acetylation influences cytoplasmic microtubule levels via the stabilization of flagellar microtubules Major achievement

Rinka Sasaki, Tomohiro Kubo, Toshiyuki Oda

2025.3

　More details

Event date： 2025.3

Language：English Presentation type：Poster presentation
チューブリンアセチル化による鞭毛軸糸の安定性制御 Major achievement

久保智広

第18回クラミドモナス研究会 2025.3

　More details

Event date： 2025.3

Language：Japanese Presentation type：Oral presentation(general)
Tubulin glycylation controls ciliary motility through modulation of outer-arm dyneins Major achievement

Tomohiro Kubo, Rinka Sasaki, and Toshiyuki Oda

2024.7

　More details

Language：English Presentation type：Poster presentation
Tubulin glycylation controls ciliary motility through modulation of outer-arm dyneins Major achievement

Tomohiro Kubo, Rinka Sasaki, Toshiyuki Oda

2024.7

　More details

Event date： 2024.7

Language：English Presentation type：Poster presentation

File： 2024_jscb.pdf
クラミドモナスの鞭毛内で見つかった蛋白質合成系の解明 Major achievement

久保智広

第13回繊毛研究会 2023.10

　More details

Language：Japanese Presentation type：Oral presentation(general)
クラミドモナスの鞭毛内で見つかった蛋白質合成系の解明 Major achievement

久保智広

第13回繊毛研究会 2023.10

　More details

Event date： 2023.10

Language：Japanese
Distinct roles of a- and b-tubulin C-terminal tails for ciliary function as revealed by a CRISPR/Cas9 mediated gene editing in Chlamydomonas Major achievement

Tomohiro Kubo, Yuma Tani, Haru-Aki Yanagisawa, Masahide Kikkawa, Toshiyuki Oda

2023.7

　More details

Language：English Presentation type：Poster presentation
Distinct roles of a- and b-tubulin C-terminal tails for ciliary function as revealed by a CRISPR/Cas9 mediated gene editing in Chlamydomonas Major achievement

Tomohiro Kubo, Yuma Tani, Haru-Aki Yanagisawa, Masahide Kikkawa, Toshiyuki Oda

The 49th Naito Conference 2023.7

　More details

Event date： 2023.7

Language：English Presentation type：Poster presentation
単細胞緑藻類クラミドモナスの繊毛で新規に見つかった蛋白質合成系の解明 Major achievement

久保智広, 小田賢幸

第75回日本細胞生物学会 2023.6

　More details

Language：Japanese Presentation type：Poster presentation

Venue：奈良県コンベンションセンター
Elucidation of a protein synthesis machinery in the cilia of the unicellular green alga Chlamydomonas Major achievement

Tomohiro Kubo, Toshiyuki Oda

2023.6

　More details

Event date： 2023.6

Language：English Presentation type：Poster presentation
Distinct roles of a- and b-tubulin C-terminal tails for ciliary function as revealed by a CRISPR/Cas9 mediated gene editing in Chlamydomonas International conference Major achievement

Tomohiro Kubo, Yuma Tani, Haru-Aki Yanagisawa, Masahide Kikkawa, Toshiyuki Oda

20th International Conference on the Cell and Molecular Biology of Chlamydomonas 2023.6

　More details

Language：English Presentation type：Poster presentation

Venue：Princeton University
Distinct roles of a- and b-tubulin C-terminal tails for ciliary function as revealed by a CRISPR/Cas9 mediated gene editing in Chlamydomonas

Tomohiro Kubo, Yuma Tani, Haru-Aki Yanagisawa, Masahide Kikkawa, Toshiyuki Oda

20th International Conference on the Cell and Molecular Biology of Chlamydomonas 2023.6

　More details

Event date： 2023.6

Language：English Presentation type：Poster presentation

Venue：Prinston University Country：United States
クラミドモナス鞭毛で新規に見つかった蛋白質合成系の解明 Major achievement

久保智広

繊毛研究会 2022.10

　More details

Event date： 2022.10

Language：Japanese Presentation type：Oral presentation(general)

Venue：名古屋市立大学
クラミドモナス鞭毛で新規に見つかった蛋白質合成系の解明 Major achievement

久保智広

第11回繊毛研究会 2022.10

　More details

Language：Japanese Presentation type：Oral presentation(general)

Venue：名古屋市立大学
SUnSET法による鞭毛構築中の新規合成蛋白質のモニタリング Major achievement

久保智広

第74回日本細胞生物学会 2022.6

　More details

Event date： 2022.6

Language：Japanese Presentation type：Oral presentation(general)

Venue：タワーホール船堀
SUnSET法による鞭毛構築中の新規合成蛋白質のモニタリング Major achievement

久保智広

第74回日本細胞生物学会 2022.6

　More details

Event date： 2022.6

Language：English Presentation type：Oral presentation(general)

Venue：タワーホール船堀
SUnSET法による鞭毛構築中の新規合成蛋白質のモニタリング Major achievement

久保智広

繊毛研究会 2021.11

　More details

Event date： 2021.11

Language：Japanese
SUnSET法による鞭毛構築中の新規合成蛋白質のモニタリング Major achievement

久保智広, 加納夏美, 小田賢幸

第11回繊毛研究会 2021.11

　More details

Language：Japanese

Venue：オンライン開催
単細胞緑藻類クラミドモナスを用いた鞭毛内輸送系蛋白質IFT38の機能解析 Major achievement

久保智広, 青田海人, 高橋光規, 加納夏実, 小田賢幸

第73回日本細胞生物学会 2021.7

　More details

Language：Japanese Presentation type：Oral presentation(general)

Venue：オンライン開催
単細胞緑藻類クラミドモナスを用いた鞭毛内輸送系蛋白質IFT38の機能解析 Major achievement

久保智広

第73回日本細胞生物学会大会 2021.6

　More details

Event date： 2021.6

Language：Japanese
チューブリンポリグルタミン酸化修飾による鞭毛繊毛の運動制御：αチューブリン改変株を用いた解析 Major achievement

久保智広

第14回クラミドモナス研究会 2021.3

　More details

Event date： 2021.3

Language：Japanese Presentation type：Poster presentation

Venue：オンライン開催
チューブリンポリグルタミン酸化修飾による鞭毛繊毛の運動制御：αチューブリン改変株を用いた解析 Major achievement

久保智広

第14回クラミドモナス研究会 2021.3

　More details

Event date： 2021.3

Language：English Presentation type：Poster presentation

Venue：オンライン開催
Ca2+ signaling surpasses the suppression of flagellar assembly in the axonemal dynein-lacking mutant Major achievement

Natsumi Kanou, Tomohiro Kubo1, and Toshiyuki Oda1

2020.9

　More details

Event date： 2020.9

Language：English Presentation type：Poster presentation
Identification of polyglutamylation sites in Chlamydomonas alpha-tubulin Major achievement

Tomohiro Kubo and Toshiyuki Oda1

2020.9

　More details

Event date： 2020.9

Language：English Presentation type：Poster presentation
カルシウムイオン依存的な鞭毛構築機構の解明

久保智広、加納夏実、小田賢幸

繊毛研究会 2019.11

　More details

Event date： 2019.11

Language：Japanese Presentation type：Oral presentation(general)

Venue：東京工業大学
カルシウムイオン依存的な鞭毛構築機構の解明 Major achievement

久保智広, 加納夏実, 小田賢幸

第10回繊毛研究会 2019.11

　More details

Event date： 2019.11

Language：Japanese

Venue：東京農工大学
Ca2+ signaling surpasses the suppression of flagellar assembly in the axonemal dynein-lacking mutant Major achievement

Natsumi Kanou, Tomohiro Kubo, Toshiyuki Oda

2019.9

　More details

Event date： 2019.9

Language：English Presentation type：Poster presentation
Identification of polyglutamylation sites in Chlamydomonas alpha-tubulin Major achievement

Tomohiro Kubo, Toshiyuki Oda

2019.9

　More details

Event date： 2019.9

Language：English Presentation type：Poster presentation
A Microtubule-Dynein Tethering Complex Regulates the Axonemal Inner Dynein f (I1) International conference Major achievement

Tomohiro Kubo

18th International Conference on the Cell and Molecular Biology of Chlamydomonas 2018.6

　More details

Event date： 2018.6

Language：English Presentation type：Oral presentation(invited, special)

Venue：Washington DC
A microtubule-dynein tethering complex regulates the axonemal inner dynein (I1)

Tomohiro Kubo, Yuqing Hou, Deborah Cochran, George Witman and Toshiyuki Oda

70th Annual Meeting of Japan Society for Cell Biology 2018.6

　More details

Event date： 2018.6

Language：English Presentation type：Poster presentation

Venue：Tokyo
A microtubule-dynein tethering complex regulates the axonemal inner dynein f (I1).

Tomohiro Kubo, Yuqing Hou, Deborah Cochran, George B. Witman, Toshiyuki Oda

2018.6

　More details

Event date： 2018.6

Language：English
The IFT81 and IFT74 N-termini together form the main module for intraflagellar transport(IFT) of tubulin Invited Major achievement

Tomohiro Kubo、Jason Brown, Karl Bellve, Branch Craige, Julie Craft, Kevin Forgarty, Karl Lechtreck, George Witman

2017.6

　More details

Event date： 2017.6

Language：Japanese Presentation type：Oral presentation(invited, special)
The IFT81 and IFT74 N-termini together form the main module for intraflagellar transport(IFT) of tubulin Invited

Tomohiro Kubo, Jason Brown, Karl Bellve, Branch Craige, Julie Craft, Kevin Forgarty, Karl Lechtreck, George Witman

2017.6

　More details

Language：Japanese Presentation type：Oral presentation(invited, special)
Structural biology of Chlamydomonas flagella Invited Major achievement

Tomohiro Kubo and Toshiyuki Oda

2017.5

　More details

Event date： 2017.5

Language：Japanese Presentation type：Oral presentation(invited, special)
Structural biology of Chlamydomonas flagella Invited

Tomohiro Kubo, Toshiyuki Oda

2017.5

　More details

Language：Japanese Presentation type：Oral presentation(invited, special)
The IFT81 and IFT74 N-termini together form the main module for intraflagellar transport(IFT) of tubulin Major achievement

Tomohiro Kubo, Jason Brown, Karl Bellve, Branch Craige, Julie Craft, Kevin Forgarty, Karl Lechtreck, George Witman

2016.11

　More details

Event date： 2016.11

Language：English Presentation type：Oral presentation(invited, special)
The IFT81 and IFT74 N-termini together form the main module for intraflagellar transport(IFT) of tubulin Invited

Tomohiro Kubo, Jason Brown, Karl Bellve, Branch Craige, Julie Craft, Kevin Forgarty, Karl Lechtreck, George Witman

2016.11

　More details

Language：English Presentation type：Oral presentation(invited, special)
Axonemal tubulin polyglutamylation deficiency suppresses flagellar shortness Major achievement

2015.9

　More details

Event date： 2015.9

Language：Japanese Presentation type：Oral presentation(general)
Axonemal tubulin polyglutamylation deficiency suppresses flagellar shortness

2015.9

　More details

Language：Japanese Presentation type：Oral presentation(general)
The IFT81 tubulin-binding domain and the IFT74 N-terminus individually are dispensable but together are crucial for flagellar assembly International conference Major achievement

Tomohiro Kubo, Jason M. Brown, Branch Craige, George B. Witman

FASEB (Biology of Cilia and Flagella) 2015.7

　More details

Language：English Presentation type：Oral presentation(general)
The IFT81 tubulin-binding domain and the IFT74 N-terminus individually are dispensable but　together are crucial for flagellar assembly International conference Major achievement

Tomohiro Kubo, Jason M. Brown, Branch Craige, and George B. Witman

FASEB (Biology of Cilia and Flagella) 2015.6

　More details

Event date： 2015.6

Language：English Presentation type：Oral presentation(general)

Venue：Snowmass, Colorado, USA
A novel Chlamydomonas IFT81 mutant reveals that the IFT81 tubulin-binding domain is not crucial for tubulin transport and flagellar assembly International conference Major achievement

Tomohiro Kubo, Jason M. Brown, George B. Witman

The American Society for Cell Biology 2014 2014.12

　More details

Event date： 2014.12

Language：English Presentation type：Poster presentation

Venue：Philadelphia, Pennsylvania, USA
A novel Chlamydomonas IFT81 mutant reveals that the IFT81 tubulin-binding domain is not crucial for tubulin transport and flagellar assembly

Tomohiro Kubo, Jason M. Brown, George B. Witman

The American Society for Cell Biology 2014 2014.12

　More details

Language：English Presentation type：Poster presentation
IFT74 is required for IFT-A/IFT-B interaction, but not for import of tubulin into flagella. International conference Major achievement

Jason M. Brown, Deborah A. Cochran, Tomohiro Kubo, and George B. Witman

16th International Conference on the Cell and Molecular Biology of　Chlamydomonas 2014.6

　More details

Event date： 2014.6

Language：English Presentation type：Oral presentation(invited, special)

Venue：Asilomer, CA, USA
Axonemal tubulin polyglutamylation modulates flagellar length by enhancing tubulin turnover at the flagellar tip International conference Major achievement

Tomohiro Kubo, Masafumi Hirono, Takumi Aikawa, Ritsu Kamiya, and George B. Witman

16th International Conference on the Cell and Molecular Biology of　Chlamydomonas 2014.6

　More details

Event date： 2014.6

Language：English Presentation type：Poster presentation

Venue：Asilomer, CA, USA
Axonemal tubulin polyglutamylation modulates flagellar length by enhancing tubulin turnover at the flagellar tip

Tomohiro Kubo, Masafumi Hirono, Takumi Aikawa, Ritsu Kamiya, George B. Witman

16th International Conference on the Cell and Molecular Biology of Chlamydomonas 2014.6

　More details

Language：English Presentation type：Poster presentation
IFT74 is required for IFT-A/IFT-B interaction, but not for import of tubulin into flagella

Jason M. Brown, Deborah A. Cochran, Tomohiro Kubo, George B. Witman

16th International Conference on the Cell and Molecular Biology of Chlamydomonas 2014.6

　More details

Language：English Presentation type：Oral presentation(general)
The N terminus of the IFT complex B protein IFT74 is required for normal flagellar import of complex A and BBS4 tracking, but not for tubulin import or flagellar assembly International conference Major achievement

Jason M. Brown, Deborah A. Cochran, Tomohiro Kubo, and George B. Witman.

The American Society for Cell Biology 2013 2013.12 The American Society for Cell Biology

　More details

Event date： 2013.12

Language：English Presentation type：Poster presentation

Venue：New Orleans, LA, USA
A suppressor mutant, ssh1, of flagellar shortness in dynein-deficient Chlamydomonas strains is　 deficient in the gene encoding FAP234, a protein involved in tubulin polyglutamylation International conference Major achievement

Tomohiro Kubo, Masafumi Hirono, Takumi Aikawa, George B. Witman, and Ritsu Kamiya

The American Society for Cell Biology 2013 2013.12 The American Society for Cell Biology

　More details

Event date： 2013.12

Language：English Presentation type：Poster presentation

Venue：New Orleans, LA, USA
A suppressor mutant, ssh1, of flagellar shortness in dynein-deficient Chlamydomonas strains is deficient in the gene encoding FAP234, a protein involved in tubulin polyglutamylation

Tomohiro Kubo, Masafumi Hirono, Takumi Aikawa, George B. Witman, Ritsu Kamiya

The American Society for Cell Biology 2013 2013.12

　More details

Language：English
The N terminus of the IFT complex B protein IFT74 is required for normal flagellar import of complex A and BBS4 tracking, but not for tubulin import or flagellar assembly

Jason M. Brown, Deborah A. Cochran, Tomohiro Kubo, George B. Witman

The American Society for Cell Biology 2013 2013.12

　More details

Language：English
Regulation of Axonemal Dynein Activity by a Conserved Tubulin Polyglutamylation System International conference Major achievement

Tomohiro Kubo, Zhongmei Liu, Takumi Aikawa, Toshiki Yagi, Masafumi Hirono, and Ritsu Kamiya

Dynein 2013 International Workshop 2013.11

　More details

Event date： 2013.11

Language：English Presentation type：Oral presentation(general)

Venue：Orbis Hall, Kobe, Japan
Regulation of Axonemal Dynein Activity by a Conserved Tubulin Polyglutamylation System Major achievement

Tomohiro Kubo, Zhongmei Liu, Takumi Aikawa, Toshiki Yagi, Masafumi Hirono, Ritsu, Kamiya

Dynein 2013 International Workshop 2013.11

　More details

Language：English
Regulation of Axonemal Dynein Activity by a Conserved Tubulin Polyglutamylation System Major achievement

Tomohiro Kubo, Zhongmei Liu, Toshiki Yagi, Masafumi Hirono, and Ritsu Kamiya

The 25th CDB Meeting; Cilia and Centrosomes: from Fertilization to Cancer 2013.6

　More details

Event date： 2013.6

Language：Japanese Presentation type：Oral presentation(general)

Venue：RIKEN CDB, Kobe, Japan
Regulation of Axonemal Dynein Activity by a Conserved Tubulin Polyglutamylation System Major achievement

Tomohiro Kubo, Zhongmei Liu, Toshiki Yagi, Masafumi Hirono, ○Ritsu Kamiya

The 25th CDB Meeting; Cilia and Centrosomes: from Fertilization to Cancer 2013.6

　More details

Language：English Presentation type：Oral presentation(general)

Venue：RIKEN CDB, Kobe, Japan
鞭毛運動のチューブリン・ポリグルタミン酸化修飾による調節 Major achievement

久保智広、八木俊樹、神谷律

生体運動班会議 2013.1

　More details

Event date： 2013.1

Language：Japanese Presentation type：Oral presentation(general)

Venue：広島大学
鞭毛運動のチューブリン・ポリグルタミン酸化修飾による調節

久保智広, 八木俊樹, 神谷律

生体運動班会議 2013.1

　More details

Language：Japanese Presentation type：Oral presentation(general)

Venue：広島大学
A novel Chlamydomonas mutant, tpg2, reveals a conserved 177-kDa protein crucial for the localization of TTLL9, an enzyme that catalyzes tubulin polyglutamylation in the axoneme International conference Major achievement

omohiro Kubo, Yanagisawa Haru-aki, Zhongmei Liu, Rie Shibuya, Masafumi Hirono, and Ritsu Kamiya

The American Society for Cell Biology 2012 2012.12 The American Society for Cell Biology

　More details

Event date： 2012.12

Language：English Presentation type：Poster presentation

Venue：San Francisco, USA
A novel Chlamydomonas mutant, tpg2, reveals a conserved 177-kDa protein crucial for the localization of TTLL9, an enzyme that catalyzes tubulin polyglutamylation in the axoneme

Tomohiro Kubo, Yanagisawa Haru-aki, Zhongmei Liu, Rie Shibuya, Masafumi Hirono, Ritsu Kamiya

The American Society for Cell Biology 2012 2012.12

　More details

Language：English Presentation type：Poster presentation
Tubulin polyglutamylation regulates axonemal motility by modulating the function of a particular inner-arm dynein species (dynein e) Major achievement

Tomohiro Kubo, Toshiki Yagi, and Ritsu Kamiya

2012.9

　More details

Event date： 2012.9

Language：English Presentation type：Poster presentation
Tubulin polyglutamylation regulates axonemal motility by modulating the function of a particular inner-arm dynein species (dynein e).

Tomohiro Kubo, Toshiki Yagi, Ritsu Kamiya

2012.9

　More details

Language：English Presentation type：Poster presentation
Tubulin polyglutamylation regulates axonemal motility by modulating the function of a particular inner-arm dynein species (dynein e). International conference Major achievement

Tomohiro Kubo, Toshiki Yagi, and Ritsu Kamiya

15th International Conference on the Cell and Molecular Biology of Chlamydomonas 2012.6

　More details

Event date： 2012.6

Language：English Presentation type：Poster presentation

Venue：Potsdam, Germany
Tubulin polyglutamylation regulates axonemal motility by modulating the function of a particular inner-arm dynein species (dynein e).

Tomohiro Kubo, Toshiki Yagi, Ritsu Kamiya

15th International Conference on the Cell and Molecular Biology of Chlamydomonas 2012.6

　More details

Language：English Presentation type：Poster presentation
Tubulin polyglutamylation regulates flagellar motility by modulating the function of inner arm dynein “e” International conference Major achievement

Tomohiro Kubo, Toshiki Yagi, and Ritsu Kamiya

The American Society for Cell Biology 2011 2011.12 The American Society for Cell Biology

　More details

Event date： 2011.12

Language：English Presentation type：Poster presentation

Venue：Colorado Convention Center, Denber, Colofado, USA
Tubulin polyglutamylation regulates flagellar motility by modulating the function of inner arm dynein “e”

Tomohiro Kubo, Toshiki Yagi, Ritsu Kamiya

The American Society for Cell Biology 2011 2011.12

　More details

Event date： 2011.12

Language：English Presentation type：Poster presentation
軸糸チューブリン・ポリグルタミン酸化修飾に関与する新規鞭毛蛋白質の同定 Major achievement

久保智広、柳澤春明、劉中美、廣野雅文、神谷律

第81回日本動物学会 2011.9 日本動物学会

　More details

Event date： 2011.9

Language：Japanese Presentation type：Oral presentation(general)

Venue：旭川市大雪クリスタルホール
Identification of a novel Chlamydomonas flagellar protein involved in tubulin polyglutamylation

2011.9

　More details

Language：Japanese Presentation type：Oral presentation(general)
Tubulin Polyglutamylation Regulates Flagellar Motility Through the Function of Dynein Regulatory Complex Major achievement

Tomohiro Kubo and Ritsu Kamiya

2011.9

　More details

Event date： 2011.9

Language：English Presentation type：Poster presentation
Tubulin Polyglutamylation Regulates Flagellar Motility Through the Function of Dynein Regulatory Complex Major achievement

Tomohiro Kubo, Ritsu Kamiya

2011.9

　More details

Language：English
A novel Chlamydomonas mutant, tpg2, reveals a conserved 177-kDa protein associated with TTLL9, an enzyme that catalyzes tubulin polyglutamylation in the axoneme Major achievement

Tomohiro Kubo, Haru-aki Yanagisawa, Zhongmei Liu, Masafumi Hirono, and Ritsu Kamiya

2011.6

　More details

Event date： 2011.6

Language：English Presentation type：Poster presentation
A novel Chlamydomonas mutant, tpg2, reveals a conserved 177-kDa protein associated with TTLL9, an enzyme that catalyzes tubulin polyglutamylation in the axoneme

Tomohiro Kubo, Haru-aki Yanagisawa, Zhongmei Liu, Masafumi Hirono, Ritsu Kamiya

2011.6

　More details

Language：English Presentation type：Poster presentation
チューブリン・ポリグルタミン酸化修飾による軸糸ダイニンと鞭毛運動の調節 Major achievement

久保智広、柳澤春明、八木俊樹、廣野雅文、神谷律

生体運動合同班会議 2010.11

　More details

Event date： 2010.11

Language：Japanese Presentation type：Oral presentation(general)

Venue：中央大学理工学部
Tubulin Polyglutamylation Regulates Flagellar Motility by Affecting Functions of Inner-Arm Dyneins Major achievement

2010.9

　More details

Event date： 2010.9

Language：English Presentation type：Poster presentation
Tubulin Polyglutamylation Regulates Flagellar Motility by Affecting Functions of Inner-Arm Dyneins Major achievement

2010.9

　More details

Event date： 2010.9

Language：English Presentation type：Poster presentation
Tubulin Polyglutamylation Regulates Flagellar Motility by Affecting Functions of Inner-Arm Dyneins Major achievement

Tomohiro Kubo, Haru-aki Yanagisawa, Toshiki Yagi, Masafumi Hirono, Ritsu Kamiya

第62回日本細胞生物学会 2010.5 日本細胞生物学会

　More details

Event date： 2010.5

Language：Japanese Presentation type：Poster presentation

Venue：大阪国際会議場
Tubulin Polyglutamylation Regulates Flagellar Motility by Affecting Functions of Inner-Arm Dyneins Major achievement

Tomohiro Kubo, Haru-aki Yanagisawa, Toshiki Yagi, Masafumi Hirono, Ritsu Kamiya

2010.5

　More details

Event date： 2010.5

Language：English Presentation type：Poster presentation
チューブリン・ポリグルタミン酸化修飾による軸糸ダイニンと鞭毛運動の調節 Major achievement

久保智広, 柳澤春明, 八木俊樹, 廣野雅文, 神谷律

生体運動合同班会議 2010.1

　More details

Event date： 2010.1

Language：Japanese

Venue：中央大学理工学部
Importance of Tubulin Polyglutamylation for Axonemal Dynein Function as Revealed by a Novel Chlamydomonas Mutant International conference Major achievement

Tomohiro Kubo, Haru-aki Yanagisawa, Toshiki Yagi, Masafumi Hirono, Ritsu Kamiya

2009.11

　More details

Event date： 2009.11

Language：English Presentation type：Poster presentation
Importance of Tubulin Polyglutamylation for Axonemal Dynein Function as Revealed by a Novel Chlamydomonas Mutant Major achievement

Tomohiro Kubo, Haru-aki Yanagisawa, Toshiki Yagi, Masafumi Hirono, Ritsu Kamiya

2009.11

　More details

Event date： 2009.11

Language：English Presentation type：Poster presentation
クラミドモナス鞭毛運動におけるチューブリン・ポリグルタミル化修飾の重要性 Major achievement

久保智広、柳澤春明、八木俊樹、廣野雅文、神谷律

第61回日本細胞生物学会 2009.6 日本細胞生物学会

　More details

Event date： 2009.6

Language：Japanese Presentation type：Poster presentation

Venue：名古屋国際会議場
クラミドモナス鞭毛運動におけるチューブリン・ポリグルタミル化修飾の重要性

久保智広, 柳澤春明, 八木俊樹, 廣野雅文, 神谷律

第61回日本細胞生物学会 2009.6 日本細胞生物学会

　More details

Event date： 2009.6

Language：Japanese Presentation type：Poster presentation

Venue：名古屋国際会議場
Importance of tubulin polyglutamylation for cilia/flagella motility as revealed by a novel a Chlamydomonas mutant International conference Major achievement

Tomohiro Kubo, Haru-aki Yanagisawa, Toshiki Yagi, Masafumi Hirono, and Ritsu Kamiya

Gordon Research Conference 2009 (Cilia, Mucus & Mucociliary Interactions) 2009.2

　More details

Event date： 2009.2

Language：English Presentation type：Poster presentation

Venue：Lucca (Barga), Italy
Importance of tubulin polyglutamylation for cilia/flagella motility as revealed by a novel Chlamydomonas mutant

Tomohiro Kubo, Haru-aki Yanagisawa, Toshiki Yagi, Masafumi Hirono, Ritsu Kamiya

Gordon Research Conference2009 (Cilia, Mucus & Mucociliary Interactions) 2009.2

　More details

Event date： 2009.2

Language：English Presentation type：Poster presentation

Venue：Lucca (Barga), Italy
クラミドモナス変異株で明らかになった鞭毛チューブリン翻訳後修飾の機能的重要性 Major achievement

久保智広、柳澤春明、八木俊樹、神谷律

日本動物学会第79回大会 2008.9 日本動物学会

　More details

Event date： 2008.9

Language：Japanese Presentation type：Oral presentation(general)

Venue：福岡大学
クラミドモナス変異株で明らかになった鞭毛チューブリン翻訳後修飾の機能的重要性

久保智広, 柳澤春明, 八木俊樹, 神谷律

日本動物学会第79回大会 2008.9 福岡大学

　More details

Event date： 2008.9

Language：Japanese Presentation type：Oral presentation(general)

▼display all

Awards

Undergraduate Poster Award Major achievement

2025.3 Tubulin acetylation influences cytoplasmic microtubule levels via the stabilization of flagellar microtubules

Rinkda Sasaki, Tomohiro Kubo, and Toshiyuki Oda

　More details

Award type：Award from Japanese society, conference, symposium, etc.
Poster Award for Excellence Major achievement

2023.7

　More details

Distinct roles of a- and b-tubulin C-terminal tails for ciliary function as revealed by a CRISPR/Cas9 mediated gene editing in Chlamydomonas
Poster Award for Excellence Major achievement

2023.7 Distinct roles of a- and b-tubulin C-terminal tails for ciliary function as revealed by a CRISPR/Cas9 mediated gene editing in Chlamydomonas

Tomohiro Kubo, Yuma Tani, Haru-Aki Yanagisawa, Masahide Kikkawa, Toshiyuki Oda

　More details

Award type：Award from international society, conference, symposium, etc.
1st place Major achievement

2014.6 16th International Conference on the Cell and Molecular Biology of Chlamydomonas. Poster award

Tomohiro Kubo
3rd place Major achievement

2012.6 15th International Conference on the Cell and Molecular Biology of Chlamydomonas. Poster award

Tomohiro Kubo

Teaching Experience (On-campus)

Gross Anatomy (Anatomy B)

2024Year
Introduction to Human Morphology and Function Major achievement

2024Year
Introduction to Human Morphology and Function Major achievement

2023Year
Life Science of the Human Body

2023Year
人体形態・機能学概論

2022Year Type of subject：Master's (Graduate School)
全学共通教育科目「人体の生命科学」

2022Year Type of subject：Common education (undergraduate)
解剖学A Major achievement

2019Year Type of subject：Common education (undergraduate)
解剖学A

2018Year Type of subject：Common education (undergraduate)
解剖学B

2018Year
解剖学A Major achievement

2017Year Type of subject：Common education (undergraduate)
分子組織学 Major achievement

2017Year Type of subject：Common education (undergraduate)

▼display all

Teaching Experience

解剖学B
解剖学A

Guidance results

2022

Type：Master's （Major B course）dissertations guidance Period：24months Year guidance time：500hours

Number of people receiving guidance ：1people
2021

Type：Master's （Major B course）dissertations guidance Period：24months Year guidance time：500hours

Number of people receiving guidance ：1people
2020

Type：Master's （Major B course）dissertations guidance Period：12months

Number of people receiving guidance ：1people

Teaching achievements

FD研修会への参加（特進コース冬季合宿の際）

2019.02.21

Review of master's and doctoral thesis

2022

Examiner classification：Second reader

Doctoral ：1people
2021

Examiner classification：Second reader

Doctoral ：1people

Professional Memberships

JAPAN SOCIETY FOR CELL BIOLOGY
THE BIOPHYSICAL SOCIETY OF JAPAN
THE ZOOLOGICAL SOCIETY OF JAPAN

Media Coverage

チューブリングリシル化は外腕ダイニンに影響を与えることによって、繊毛の運動性を調節する Internet

ユサコ株式会社国内研究者論文詳細 2024.6

　More details

Author：Myself