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チバ　キヨウコ

千葉　杏子

Kyoko Chiba

所属

高等研究機構学際科学フロンティア研究所　新領域創成研究部学際基盤研究分野　生命・環境研究領域

職名

助教

学位

博士（薬科学）（北海道大学）

researchmap

https://researchmap.jp/kchiba

J-GLOBAL ID

201301006214300400

e-Rad 研究者番号

10795701

ORCID

https://orcid.org/0000-0001-6919-2782

プロフィール

2016年に北海道大学にて博士（薬科学）の学位を取得後、カリフォルニア大学デービス校生物科学部（Richard McKenney Lab）において、モータータンパク質の生化学および生物物理学の研究に従事しました。2021年、文部科学省卓越研究員として東北大学学際科学フロンティア研究所テニュアトラック助教に着任しました。

「ニューロンはいかにしてその健康を維持し続けるのか」という問いを研究の核心に据え、分子モーターおよび細胞骨格を中心とした研究を進めています。これまで、キネシンタンパク質の活性制御機構と、その破綻によって生じる神経変性疾患の分子基盤の解明に取り組んできました。特に、軸索輸送の障害がALSをはじめとする運動ニューロン疾患の発症にどのように関与するのか明らかにすることを目指しています。

基礎研究から得られた知見を将来の治療戦略へとつなげることで、神経難病の克服に貢献することを目標としています。

経歴 5

2021年4月～継続中

東北大学学際科学フロンティア研究所助教
2021年1月～ 2025年3月

文部科学省卓越研究員
2017年6月～ 2021年3月

カリフォルニア大学デービス校（Richard McKenney 研究室）博士研究員
2016年4月～ 2017年3月

北海道大学薬学部（鈴木利治研究室）日本学術振興会特別研究員PD
2017年4月～ 2017年5月

北海道大学薬学部（鈴木利治研究室）博士研究員

学歴 3

北海道大学大学院生命科学院生命科学専攻博士後期課程

2013年4月～ 2016年3月
北海道大学大学院生命科学院生命科学専攻修士課程

2011年4月～ 2013年3月
北海道大学薬学部薬科学科

2007年4月～ 2011年3月

研究分野 1

ライフサイエンス / 機能生物化学 /

受賞 11

東北大学優秀女性研究者賞「紫千代萩賞」

2025年3月
WILEY Top Cited Article 2022-2023

2024年4月
WILEY Top Downloaded Article 2022

2024年3月
WILEY Top Cited Article 2021-2022

2023年2月
第60回日本生物物理学会若手招待講演賞

2022年9月
日本生化学会北海道支部若手奨励賞

2017年7月
北海道大学大塚賞

2016年3月
第42回日本分子生物学会海外若手会員招聘企画（トラベルアワード）

2019年12月
早石修記念海外留学助成

2018年6月
American Society for Cell Biology, International Travel Award

2016年12月
第86回日本生化学会大会鈴木紘一メモリアル賞

2013年9月

︎全件表示 ︎最初の5件までを表示

論文 22

Activated kinesin-1 assembles into a dimer-of-dimers

Kyoko Chiba

bioRxiv　2025年12月26日

DOI： 10.64898/2025.12.23.696152 　
Protocol for Reconstituting Adaptor‐Mediated Activation of Full‐Length Kinesin‐1 査読有り

Haruka Masumoto, Kyoko Chiba

Cytoskeleton　2025年12月5日
出版者・発行元： Wiley
DOI： 10.1002/cm.70079 　

ISSN：1949-3584

eISSN：1949-3592

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ABSTRACT Kinesin‐1 is a member of the kinesin superfamily that plays an essential role in intracellular cargo transport. In the absence of cargo, Kinesin‐1 exhibits low motor activity due to autoinhibition. Multiple studies have demonstrated that adaptor proteins, which link cargos to Kinesin‐1, can activate Kinesin‐1 by releasing the autoinhibition. To elucidate the molecular mechanism of adaptor‐mediated activation, in vitro reconstitution of the Kinesin‐1 complex has proven to be a powerful approach. We have shown that the binding of an adaptor protein, Nesprin‐4, is sufficient to activate Kinesin‐1 motility in vitro. Here, we present protocols for the observation and assessment of adaptor‐mediated Kinesin‐1 activation. Using C. elegans and human Kinesin‐1 as examples, we describe steps and critical considerations for preparing the Kinesin‐1 complex. We also detail how to mix it with an adaptor protein and visualize the resulting motility using total internal reflection fluorescence (TIRF) microscopy. Finally, we describe analytical methods for assessing motor activation. This protocol will be valuable for future studies aiming to evaluate the activation of Kinesin‐1 by known or unknown activator molecules.
Kinesins in Caenorhabditis elegans neuronal morphogenesis 招待有り査読有り

Shinsuke Niwa, Kyoko Chiba

Open Biology　2025年11月

DOI： 10.1098/rsob.250072 　
The KASH protein UNC-83 differentially regulates kinesin-1 activity to control developmental stage-specific nuclear migration 査読有り

Selin Gümüşderelioğlu, Natalie Sahabandu, Daniel Elnatan, Ellen F. Gregory, Kyoko Chiba, Shinsuke Niwa, G.W. Gant Luxton, Richard J. McKenney, Daniel A. Starr

Current Biology　2025年9月
出版者・発行元： Elsevier BV
DOI： 10.1016/j.cub.2025.08.025 　

ISSN：0960-9822
The chromokinesin Kid (KIF22) forms a homodimer, moves processively along microtubules and transports double-strand DNA 査読有り

Shinsuke Niwa, Natsuki Furusaki, Tomoki Kita, Yuki Suzuki, Kyoko Chiba

eLife　2024年11月19日
出版者・発行元： eLife Sciences Publications, Ltd
DOI： 10.7554/elife.102828.1 　

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During prometaphase in mitosis, chromosomes are pushed toward the spindle equator. The chromokinesin Kid, also known as KIF22, moves chromosomes along spindle microtubules during prometaphase. Kid has long been considered as a monomeric and non-processive motor, different from typical kinesins. In this study, we demonstrate that the full-length Kid forms a homodimer and moves processively along microtubules. A conserved coiled-coil domain within the stalk region of Kid is not only capable of homodimer formation, but is also required for the processivity of Kid. Furthermore, the neck linker and coiled-coil domains of Kid could add processive activity to the motor domain of KIF1A, suggesting that Kid contains a functional neck linker and dimerization capability, a prerequisite for the processivity of kinesin motor domains. The full-length Kid, containing a helix-hairpin-helix domain, can transport double-strand DNA along microtubules in vitro. These findings collectively suggest the reclassification of Kid as a processive motor that transports DNA along microtubules.
Characterizing human KIF1Bß motor activity by single-molecule motility assays and Caenorhabtidis elegans genetics 査読有り

Rei Iguchi, Tomoki Kita, Taisei Watanabe, Kyoko Chiba, Shinsuke Niwa

Journal of Cell Science　2024年9月16日
出版者・発行元： The Company of Biologists
DOI： 10.1242/jcs.261783 　

ISSN：0021-9533

eISSN：1477-9137

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The axonal transport of synaptic vesicle precursors relies on KIF1A and UNC-104 ortholog motors. In mammals, KIF1Bß is also responsible for the axonal transport of synaptic vesicle precursors. Mutations in KIF1A and KIF1Bß lead to a wide range of neuropathies. While previous studies have revealed the biochemical, biophysical and cell biological properties of KIF1A, and its defects in neurological disorders, the fundamental properties of KIF1Bß remain elusive. In this study, we determined the motile parameters of KIF1Bß through single-molecule motility assays. We find that the C-terminal region of KIF1Bß has an inhibitory role in the motor activity. Alphafold2 prediction suggests that the C-terminal region blocks the motor domain. Additionally, we established simple methods for testing the axonal transport activity of human KIF1Bß using Caenorhabditis elegans genetics. Taking advantage of these methods, we demonstrated that these assays enable the detection of reduced KIF1Bß activities both in vitro and in vivo, that is caused by a Charcot-Marie-Tooth-disease-associated Q98L mutation.
The FHA domain is essential for the autoinhibition of KIF1A/UNC-104 査読有り

Shinsuke Niwa, Taisei Watanabe, Kyoko Chiba

Journal of Cell Science　2024年9月6日
出版者・発行元： The Company of Biologists
DOI： 10.1242/jcs.262017 　

ISSN：0021-9533

eISSN：1477-9137

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KIF1A/UNC-104, a member of the kinesin superfamily motor proteins, plays a pivotal role in the axonal transport of synaptic vesicles and their precursors. Drosophila melanogaster UNC-104 (DmUNC-104) is a relatively recently discovered Drosophila kinesin. Although some point mutations that disrupt synapse formation have been identified, the biochemical properties of DmUNC-104 protein have not been investigated. Here, we prepared recombinant full-length DmUNC-104 protein and determined its biochemical features. We analyzed the effect of a previously identified missense mutation in the forkhead-associated (FHA) domain, called bristly (bris). The bris mutation strongly promoted the dimerization of DmUNC-104 protein, whereas wild-type DmUNC-104 was a mixture of monomers and dimers. We further tested the G618R mutation near the FHA domain which was previously shown to disrupt the autoinhibition of C. elegans UNC-104. The biochemical properties of the G618R mutant recapitulated those of the bris mutant. Finally, we found that disease-associated mutations also promote the dimerization of DmUNC-104. Collectively, our results suggest that the FHA domain is essential for the autoinhibition of KIF1A/UNC-104, and that abnormal dimerization of KIF1A is linked to human diseases.
Autoinhibition and activation of kinesin-1 and their involvement in amyotrophic lateral sclerosis 招待有り査読有り

Kyoko Chiba, Shinsuke Niwa

Current Opinion in Cell Biology　86　102301-102301　2024年2月
出版者・発行元： Elsevier BV
DOI： 10.1016/j.ceb.2023.102301 　

ISSN：0955-0674
Comparative analysis of two Caenorhabditis elegans kinesins KLP-6 and UNC-104 reveals a common and distinct activation mechanism in kinesin-3 査読有り

Tomoki Kita, Kyoko Chiba, Jiye Wang, Atsushi Nakagawa, Shinsuke Niwa

eLife　12　2024年1月11日
出版者・発行元： eLife Sciences Publications, Ltd
DOI： 10.7554/elife.89040 　

eISSN：2050-084X

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Kinesin-3 is a family of microtubule-dependent motor proteins that transport various cargos within the cell. However, the mechanism underlying kinesin-3 activations remains largely elusive. In this study, we compared the biochemical properties of two Caenorhabditis elegans kinesin-3 family proteins, KLP-6 and UNC-104. Both KLP-6 and UNC-104 are predominantly monomeric in solution. As previously shown for UNC-104, non-processive KLP-6 monomer is converted to a processive motor when artificially dimerized. We present evidence that releasing the autoinhibition is sufficient to trigger dimerization of monomeric UNC-104 at nanomolar concentrations, which results in processive movement of UNC-104 on microtubules, although it has long been thought that enrichment in the phospholipid microdomain on cargo vesicles is required for the dimerization and processive movement of UNC-104. In contrast, KLP-6 remains to be a non-processive monomer even when its autoinhibition is unlocked, suggesting a requirement of other factors for full activation. By examining the differences between KLP-6 and UNC-104, we identified a coiled-coil domain called coiled-coil 2 (CC2) that is required for the efficient dimerization and processive movement of UNC-104. Our results suggest a common activation mechanism for kinesin-3 family members, while also highlighting their diversification.
Generation of recombinant and chickenized scFv versions of an anti-kinesin monoclonal antibody H2. 国際誌査読有り

Shinsuke Niwa, Kyoko Chiba

Cytoskeleton　2023年4月10日

DOI： 10.1002/cm.21756 　

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Kinesin-1, a motor protein composed of the kinesin heavy chain (KHC) and the kinesin light chain (KLC), is essential for proper cellular morphogenesis and function. A monoclonal antibody (mAb) called H2 recognizes the KHC in a broad range of species and is one of the most widely used mAbs in cytoskeletal motor research. Here, we present vectors that express recombinant H2 in mammalian cells. We show the recombinant H2 performs as well as the hybridoma-derived H2 in both western blotting and immunofluorescence assays. Additionally, the recombinant H2 can detect all three human KHC isotypes (KIF5A, KIF5B, and KIF5C) and amyotrophic lateral sclerosis-associated KIF5A aggregates in cells. In addition, we developed a chickenized version of the H2 mAb's single chain variable fragment, which can be used in immunofluorescence microscopy and expands the potential applications of H2. Overall, our results demonstrate that recombinant H2 is a useful tool for studying the functions of KHCs.
Insight into the regulation of axonal transport from the study of KIF1A-associated neurological disorder 招待有り査読有り

Kyoko Chiba, Tomoki Kita, Yuzu Anazawa, Shinsuke Niwa

Journal of Cell Science　136　(5)　2023年1月19日
出版者・発行元： The Company of Biologists
DOI： 10.1242/jcs.260742 　

ISSN：0021-9533

eISSN：1477-9137

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ABSTRACT Neuronal function depends on axonal transport by kinesin superfamily proteins (KIFs). KIF1A is the molecular motor that transports synaptic vesicle precursors, synaptic vesicles, dense core vesicles and active zone precursors. KIF1A is regulated by an autoinhibitory mechanism; many studies, as well as the crystal structure of KIF1A paralogs, support a model whereby autoinhibited KIF1A is monomeric in solution, whereas activated KIF1A is dimeric on microtubules. KIF1A-associated neurological disorder (KAND) is a broad-spectrum neuropathy that is caused by mutations in KIF1A. More than 100 point mutations have been identified in KAND. In vitro assays show that most mutations are loss-of-function mutations that disrupt the motor activity of KIF1A, whereas some mutations disrupt its autoinhibition and abnormally hyperactivate KIF1A. Studies on disease model worms suggests that both loss-of-function and gain-of-function mutations cause KAND by affecting the axonal transport and localization of synaptic vesicles. In this Review, we discuss how the analysis of these mutations by molecular genetics, single-molecule assays and force measurements have helped to reveal the physiological significance of KIF1A function and regulation, and what physical parameters of KIF1A are fundamental to axonal transport.
Synergistic autoinhibition and activation mechanisms control kinesin-1 motor activity. 国際誌査読有り

Kyoko Chiba, Kassandra M Ori-McKenney, Shinsuke Niwa, Richard J McKenney

Cell reports　39　(9)　110900-110900　2022年5月31日

DOI： 10.1016/j.celrep.2022.110900 　

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Kinesin-1 activity is regulated by autoinhibition. Intramolecular interactions within the kinesin heavy chain (KHC) are proposed to be one facet of motor regulation. The KHC also binds to the kinesin light chain (KLC), which has been implicated in both autoinhibition and activation of the motor. We show that the KLC inhibits the kinesin-microtubule interaction independently from the proposed intramolecular interaction within KHC. Cargo-adaptor proteins that bind the KLC stimulated processive movement, but the landing rate of activated kinesin complexes remained low. Mitogen-activated protein 7 (MAP7) enhanced motility by increasing the landing rate and run length of the activated kinesin motors. Our results support a model whereby the motor activity of the kinesin is regulated by synergistic inhibition mechanisms and that cargo-adaptor binding to the KLC releases both mechanisms. However, a non-motor MAP is required for robust microtubule association of the activated motor. Thus, human kinesin is regulated by synergistic autoinhibition and activation mechanisms.
An ALS-associated KIF5A mutant forms oligomers and aggregates and induces neuronal toxicity. 国際誌査読有り

Juri Nakano, Kyoko Chiba, Shinsuke Niwa

Genes to cells　27　(6)　421-435　2022年4月17日

DOI： 10.1111/gtc.12936 　

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KIF5A is a kinesin superfamily motor protein that transports various cargos in neurons. Mutations in Kif5a cause familial amyotrophic lateral sclerosis (ALS). These ALS mutations are in the intron of Kif5a and induce mis-splicing of KIF5A mRNA, leading to splicing out of exon 27, which in human KIF5A encodes the cargo-binding tail domain of KIF5A. Therefore, it has been suggested that ALS is caused by loss of function of KIF5A. However, the precise mechanisms regarding how mutations in KIF5A cause ALS remain unclear. Here, we show that an ALS-associated mutant of KIF5A, KIF5A(Δexon27), is predisposed to form oligomers and aggregates in cultured mouse cell lines. Interestingly, purified KIF5A(Δexon27) oligomers showed more active movement on microtubules than wild-type KIF5A in vitro. Purified KIF5A(∆exon27) was prone to form aggregates in vitro. Moreover, KIF5A(Δexon27)-expressing Caenorhabditis elegans neurons showed morphological defects. These data collectively suggest that ALS-associated mutations of KIF5A are toxic gain-of-function mutations rather than simple loss-of-function mutations.
A highly conserved 3 ₁₀ helix within the kinesin motor domain is critical for kinesin function and human health 国際誌査読有り

Aileen J. Lam, Lu Rao, Yuzu Anazawa, Kyoko Okada, Kyoko Chiba, Mariah Dacy, Shinsuke Niwa, Arne Gennerich, Dan W. Nowakowski, Richard J. McKenney

Science Advances　7　(18)　2021年4月30日
出版者・発行元： American Association for the Advancement of Science (AAAS)
DOI： 10.1126/sciadv.abf1002 　

eISSN：2375-2548

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An uncharacterized structural element in the kinesin motor domain is shown to be critical for motor function and human health.
Temperature-dependent activity of kinesins is regulable 査読有り

F. Doval, K. Chiba, R.J. McKenney, K.M. Ori-McKenney, M.D. Vershinin

Biochemical and Biophysical Research Communications　528　(3)　528-530　2020年7月
出版者・発行元： Elsevier BV
DOI： 10.1016/j.bbrc.2020.05.157 　

ISSN：0006-291X
Disease-associated mutations hyperactivate KIF1A motility and anterograde axonal transport of synaptic vesicle precursors 査読有り

Kyoko Chiba, Hironori Takahashi, Min Chen, Hiroyuki Obinata, Shogo Arai, Koichi Hashimoto, Toshiyuki Oda, Richard J. McKenney, Shinsuke Niwa

Proceedings of the National Academy of Sciences　116　(37)　18429-18434　2019年9月10日
出版者・発行元： Proceedings of the National Academy of Sciences
DOI： 10.1073/pnas.1905690116 　

ISSN：0027-8424

eISSN：1091-6490
The cytoplasmic region of the amyloid β‐protein precursor ( APP ) is necessary and sufficient for the enhanced fast velocity of APP transport by kinesin‐1 国際誌査読有り

Maoko Tsukamoto, Kyoko Chiba, Yuriko Sobu, Yuzuha Shiraki, Yuka Okumura, Saori Hata, Akira Kitamura, Tadashi Nakaya, Seiichi Uchida, Masataka Kinjo, Hidenori Taru, Toshiharu Suzuki

FEBS Letters　592　(16)　2716-2724　2018年8月
出版者・発行元： Wiley
DOI： 10.1002/1873-3468.13204 　

ISSN：0014-5793

eISSN：1873-3468

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Amyloid β-protein precursor (APP) is transported mainly by kinesin-1 and at a higher velocity than other kinesin-1 cargos, such as Alcadein α (Alcα); this is denoted by the enhanced fast velocity (EFV). Interaction of the APP cytoplasmic region with kinesin-1, which is essential for EFV transport, is mediated by JNK-interacting protein 1 (JIP1). To determine the roles of interactions between the APP luminal region and cargo components, we monitored transport of chimeric cargo receptors, Alcα (luminal)-APP (cytoplasmic) and APP (luminal)-Alcα (cytoplasmic). Alcα-APP is transported at the EFV, whereas APP-Alcα is transported at the same velocity as wild-type Alcα. Thus, the cytoplasmic region of APP is necessary and sufficient for the EFV of APP transport by kinesin-1.
Phosphorylation of KLC1 modifies interaction with JIP1 and abolishes the enhanced fast velocity of APP transport by kinesin-1 国際誌査読有り

Kyoko Chiba, Ko-yi Chien, Yuriko Sobu, Saori Hata, Shun Kato, Tadashi Nakaya, Yasushi Okada, Angus C. Nairn, Masataka Kinjo, Hidenori Taru, Rong Wang, Toshiharu Suzuki

Molecular Biology of the Cell　28　(26)　3857-3869　2017年12月15日
出版者・発行元： American Society for Cell Biology (ASCB)
DOI： 10.1091/mbc.e17-05-0303 　

ISSN：1059-1524

eISSN：1939-4586

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In neurons, amyloid β-protein precursor (APP) is transported by binding to kinesin-1, mediated by JNK-interacting protein 1b (JIP1b), which generates the enhanced fast velocity (EFV) and efficient high frequency (EHF) of APP anterograde transport. Previously, we showed that EFV requires conventional interaction between the JIP1b C-terminal region and the kinesin light chain 1 (KLC1) tetratricopeptide repeat, whereas EHF requires a novel interaction between the central region of JIP1b and the coiled-coil domain of KLC1. We found that phosphorylatable Thr466 of KLC1 regulates the conventional interaction with JIP1b. Substitution of Glu for Thr466 abolished this interaction and EFV, but did not impair the novel interaction responsible for EHF. Phosphorylation of KLC1 at Thr466 increased in aged brains, and JIP1 binding to kinesin-1 decreased, suggesting that APP transport is impaired by aging. We conclude that phosphorylation of KLC1 at Thr466 regulates the velocity of transport of APP by kinesin-1 by modulating its interaction with JIP1b.
Quantitative analysis of APP axonal transport in neurons: role of JIP1 in enhanced APP anterograde transport. 国際誌査読有り

Kyoko Chiba, Masahiko Araseki, Keisuke Nozawa, Keiko Furukori, Yoichi Araki, Takahide Matsushima, Tadashi Nakaya, Saori Hata, Yuhki Saito, Seiichi Uchida, Yasushi Okada, Angus C Nairn, Roger J Davis, Tohru Yamamoto, Masataka Kinjo, Hidenori Taru, Toshiharu Suzuki

Molecular biology of the cell　25　(22)　3569-80　2014年11月5日

DOI： 10.1091/mbc.E14-06-1111 　

ISSN：1059-1524

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Alzheimer's β-amyloid precursor protein (APP) associates with kinesin-1 via JNK-interacting protein 1 (JIP1); however, the role of JIP1 in APP transport by kinesin-1 in neurons remains unclear. We performed a quantitative analysis to understand the role of JIP1 in APP axonal transport. In JIP1-deficient neurons, we find that both the fast velocity (∼2.7 μm/s) and high frequency (66%) of anterograde transport of APP cargo are impaired to a reduced velocity (∼1.83 μm/s) and a lower frequency (45%). We identified two novel elements linked to JIP1 function, located in the central region of JIP1b, that interact with the coiled-coil domain of kinesin light chain 1 (KLC1), in addition to the conventional interaction of the JIP1b 11-amino acid C-terminal (C11) region with the tetratricopeptide repeat of KLC1. High frequency of APP anterograde transport is dependent on one of the novel elements in JIP1b. Fast velocity of APP cargo transport requires the C11 domain, which is regulated by the second novel region of JIP1b. Furthermore, efficient APP axonal transport is not influenced by phosphorylation of APP at Thr-668, a site known to be phosphorylated by JNK. Our quantitative analysis indicates that enhanced fast-velocity and efficient high-frequency APP anterograde transport observed in neurons are mediated by novel roles of JIP1b.
Simple and Direct Assembly of Kymographs from Movies Using KYMOMAKER 査読有り

Kyoko Chiba, Yuki Shimada, Masataka Kinjo, Toshiharu Suzuki, Seiich Uchida

Traffic　15　(1)　1-11　2014年1月
出版者・発行元： Wiley
DOI： 10.1111/tra.12127 　

ISSN：1398-9219
Phosphorylation of multiple sites within an acidic region of Alcadein α is required for kinesin-1 association and Golgi exit of Alcadein α cargo 国際誌査読有り

Yuriko Sobu, Keiko Furukori, Kyoko Chiba, Angus C. Nairn, Masataka Kinjo, Saori Hata, Toshiharu Suzuki

Molecular Biology of the Cell　28　(26)　3844-3856　2017年12月15日
出版者・発行元： American Society for Cell Biology (ASCB)
DOI： 10.1091/mbc.e17-05-0301 　

ISSN：1059-1524

eISSN：1939-4586

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Alcadein α (Alcα) is a major cargo of kinesin-1 that is subjected to anterograde transport in neuronal axons. Two tryptophan- and aspartic acid-containing (WD) motifs located in its cytoplasmic domain directly bind the tetratricopeptide repeat (TPR) motifs of the kinesin light chain (KLC), which activate kinesin-1 and recruit kinesin-1 to Alcα cargo. We found that phosphorylation of three serine residues in the acidic region located between the two WD motifs is required for interaction with KLC. Phosphorylation of these serine residues may alter the disordered structure of the acidic region to induce direct association with KLC. Replacement of these serines with Ala results in a mutant that is unable to bind kinesin-1, which impairs exit of Alcα cargo from the Golgi. Despite this deficiency, the compromised Alcα mutant was still transported, albeit improperly by vesicles following missorting of the Alcα mutant with amyloid β-protein precursor (APP) cargo. This suggests that APP partially compensates for defective Alcα in anterograde transport by providing an alternative cargo receptor for kinesin-1.
Facilitation of brain mitochondrial activity by 5-aminolevulinic acid in a mouse model of Alzheimer's disease. 国際誌査読有り

Chiori Omori, Rika Motodate, Yuzuha Shiraki, Kyoko Chiba, Yuriko Sobu, Ayano Kimura, Tadashi Nakaya, Hikaru Kondo, Satoshi Kurumiya, Toru Tanaka, Kazuo Yamamoto, Motowo Nakajima, Toshiharu Suzuki, Saori Hata

Nutritional neuroscience　20　(9)　538-546　2017年11月

DOI： 10.1080/1028415X.2016.1199114 　

ISSN：1028-415X

eISSN：1476-8305

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講演・口頭発表等 19

How pathogenic mutations disrupt kinesin regulation 国際会議招待有り

Kyoko Chiba

ゴードン会議 Gordon Research Conference "Cytoskeletal Motors"
Cell Biological and Biophysical Characterization of ALS-Associated KIF5A Mutant 国際会議招待有り

Kyoko Chiba

韓国分子細胞生物学会（ICKSMCB 2025）　2025年9月30日
キネシンモータータンパク質の機能異常と神経変性疾患招待有り

千葉杏子

第七回三融会・武田神経科学シンポジウム　2025年4月20日
Biochemical and Biophysical Analysis of ALS-associated KIF5A mutant 国際会議招待有り

千葉杏子

米国生物物理学会第69回年会（BPS2025）"Motility & Cytoskeleton" サブグループシンポジウム　2025年2月15日
Kinesin-3 の分子内相互作用と自己阻害招待有り

千葉杏子

第12回分子モーター討論会　2023年9月28日
KIF5A のALS 関連遺伝子変異はKIF5A のオリゴマー化と凝集を促進し神経毒性を引き起こす招待有り

千葉杏子

第60回日本生物物理学会　2022年9月28日
In Vitro Reconstitution of Kinesin-1 Activation 招待有り

千葉杏子

第59回日本生物物理学会 Japan-US symposium on cytoskeletal motor proteins and their associated proteins　2021年11月25日
Aggregation-Inducing Region of ALS-Associated KIF5A Mutant 国際会議

2024 ASCB Annual Meeting「Cell Bio 2024」　2024年12月16日
Molecular mechanisms of the ALS-associated KIF5A aggregation 国際会議

千葉杏子

EMBO・COB ワークショップ「Axonal Degeneration and Regeneration」　2024年10月9日
UNC-104 の自己阻害と２量体化

第13回分子モーター討論会　2024年9月30日
Molecular mechanisms of the ALS-associated KIF5A aggregation 国際会議

千葉杏子

ゴードンカンファレンス「Cytoskeletal Motors」　2024年7月8日
The prominent role of the FHA domain in the autoinhibition of KIF1A/UNC-104 国際会議

千葉杏子

EMBO・EMBLシンポジウム「Microtubules: from atoms to complex systems」　2024年6月7日
The FHA domain is essential for the autoinhibition of KIF1A 国際会議

Kyoko Chiba, Shinsuke Niwa

2023 ASCB Annual Meeting 「Cell Bio 2023」　2023年12月5日
KIF1A and KIF1Bβ form a heterodimer 国際会議

Kyoko CHIBA, Shinsuke NIWA

第49回内藤コンファレンス「Frontiers of Microtubule and Its-Related Motors - Atomic Structures, Cellular Functions, Development and Diseases - 」　2023年7月5日
An ALS-associated KIF5A mutant forms oligomers and aggregates and induces neuronal toxicity

Kyoko Chiba, Juri Nakano, Shinsuke Niwa

2022 ASCB Annual Meeting「Cell Bio 2022」　2022年12月6日
In vitro reconstitution of a coordinated Kinesin-1 activation

千葉杏子

第22回日本蛋白質科学会　2022年6月9日
MAP7とNesprin-4の協調によるKinesin-1活性化

千葉杏子

第44回日本分子生物学会年会　2021年12月1日
Disease-associated mutations in human KIF1A overactivate motility of KIF1A and anterograde axonal transport of synaptic vesicle precursors

千葉杏子

第42回日本分子生物学会　2019年12月5日
Single molecule analysis of the Kinesin activation

千葉杏子

東北大学国際交流セミナー　2019年11月29日

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