Updated on 2025/01/09

Information

 

写真a

 
MATSUZAWA KENJI
 
Organization
Faculty of Medical Sciences Department of Basic Medicine Lecturer
School of Sciences Department of Biology(Concurrent)
Graduate School of Systems Life Sciences Department of Systems Life Sciences(Concurrent)
Title
Lecturer
Contact information
メールアドレス
Tel
0928024294
Profile
研究及び学部生、大学院生の指導

Degree

  • PhD

Research Interests・Research Keywords

  • Research theme: Mutual regulation between force and biochemical signaling at cell-cell adhesion in epithelial cells

    Keyword: cell-cell adhesion, actomyosin cytoskeleton, signal transduction, cell communication

    Research period: 2017.6

Papers

  • MAGIs regulate aPKC to enable balanced distribution of intercellular tension for epithelial sheet homeostasis. International journal

    Kenji Matsuzawa, #Hayato Ohga, Kenta Shigetomi, @Tomohiro Shiiya, @Masanori Hirashima, Junichi Ikenouchi

    Communications Biology   4 ( 1 )   337 - 337   2021.3

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    Language:English   Publishing type:Research paper (scientific journal)  

    Constriction of the apical plasma membrane is a hallmark of epithelial cells that underlies cell shape changes in tissue morphogenesis and maintenance of tissue integrity in homeostasis. Contractile force is exerted by a cortical actomyosin network that is anchored to the plasma membrane by the apical junctional complexes (AJC). In this study, we present evidence that MAGI proteins, structural components of AJC whose function remained unclear, regulate apical constriction of epithelial cells through the Par polarity proteins. We reveal that MAGIs are required to uniformly distribute Partitioning defective-3 (Par-3) at AJC of cells throughout the epithelial monolayer. MAGIs recruit ankyrin-repeat-, SH3-domain- and proline-rich-region-containing protein 2 (ASPP2) to AJC, which modulates Par-3-aPKC to antagonize ROCK-driven contractility. By coupling the adhesion machinery to the polarity proteins to regulate cellular contractility, we propose that MAGIs play essential and central roles in maintaining steady state intercellular tension throughout the epithelial cell sheet.

    DOI: 10.1038/s42003-021-01874-z

  • α-Catenin Controls the Anisotropy of Force Distribution at Cell-Cell Junctions during Collective Cell Migration. Reviewed International journal

    Kenji Matsuzawa, #Takuya Himoto, #Yuki Mochizuki, Junichi Ikenouchi

    Cell reports   23 ( 12 )   3447 - 3456   2018.6

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    Language:English   Publishing type:Research paper (scientific journal)  

    Adherens junctions (AJs) control epithelial cell behavior, such as collective movement and morphological changes, during development and in disease. However, the molecular mechanism of AJ remodeling remains incompletely understood. Here, we report that the conformational activation of α-catenin is the key event in the dynamic regulation of AJ remodeling. α-catenin activates RhoA to increase actomyosin contractility at cell-cell junctions. This leads to the stabilization of activated α-catenin, in part through the recruitment of the actin-binding proteins, vinculin and afadin. In this way, α-catenin regulates force sensing, as well as force transmission, through a Rho-mediated feedback mechanism. We further show that this is important for stable directional alignment of multiple cells during collective cell movement by both experimental observation and mathematical modeling. Taken together, our findings demonstrate that α-catenin controls the establishment of anisotropic force distribution at cell junctions to enable cooperative movement of the epithelial cell sheet.

    DOI: 10.1016/j.celrep.2018.05.070

  • A sustained calcium response mediated by IP3 receptor anchoring to the desmosome is essential for apoptotic cell elimination.

    Cho Y, Koyama-Honda I, Tanimura A, Matsuzawa K, Ikenouchi J

    Current biology : CB   2024.9   ISSN:0960-9822

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    Language:English  

    DOI: 10.1016/j.cub.2024.08.057

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  • タイトジャンクション形成においてコレステロールの集積が果たす役割の解明

    重富 健太, 小野 由美子, 松沢 健司, 池ノ内 順一

    脂質生化学研究   65   213 - 215   2023.5   ISSN:0285-1520

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    Language:Japanese   Publisher:日本脂質生化学会  

    上皮細胞に存在するタイトジャンクション(TJ)と呼ばれる構造は、上皮細胞のバリア機能を担う。TJは、細胞接着分子クローディンが、裏打ちタンパク質ZOと結合を介して形質膜上で集積することで形成されるという仮説が広く受け入れられてきた。この仮説は、アドヘレンスジャンクション(AJ)と呼ばれるカドヘリンを介した別の接着機構からの類推に基づいており、その妥当性は検証されていない。私たちは、以前にTJ領域にコレステロールが高度に集積していることを報告した(Shigetomi et al.J.Cell Biol.,2018)。本研究では、クローディンの集積において、ZOタンパク質との結合ではなく、コレステロールに富む膜ドメインとの相互作用が重要であることを見出した。クローディンの発現を全て消失させた細胞において、ZOタンパク質と結合しないクローディン変異体を発現させた場合でも依然としてTJが形成される一方で、コレステロールに富む膜ドメインとの相互作用に必要なパルミトイル化修飾を消失させたクローディン変異体はTJを形成できないことが明らかになった。以上の結果から、TJの形成機構は、AJの形成機構とは異なり、コレステロールの集積したドメインがTJ形成において重要な役割を果たしていること、また、ZOタンパク質が細胞接着領域にコレステロールを集積させる機能を有していることが明らかになった。(著者抄録)

  • Cholesterol-rich domain formation mediated by ZO proteins is essential for tight junction formation. International journal

    Kenta Shigetomi, Yumiko Ono, Kenji Matsuzawa, Junichi Ikenouchi

    Proceedings of the National Academy of Sciences of the United States of America   120 ( 8 )   e2217561120   2023.2   ISSN:0027-8424 eISSN:1091-6490

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:Proceedings of the National Academy of Sciences of the United States of America  

    Tight junctions (TJs) are cell-adhesion structures responsible for the epithelial barrier. We reported that accumulation of cholesterol at the apical junctions is required for TJ formation [K. Shigetomi, Y. Ono, T. Inai, J. Ikenouchi, J. Cell Biol. 217, 2373-2381 (2018)]. However, it is unclear how cholesterol accumulates and informs TJ formation-and whether cholesterol enrichment precedes or follows the assembly of claudins in the first place. Here, we established an epithelial cell line (claudin-null cells) that lacks TJs by knocking out claudins. Despite the lack of TJs, cholesterol normally accumulated in the vicinity of the apical junctions. Assembly of claudins at TJs is thought to require binding to zonula occludens (ZO) proteins; however, a claudin mutant that cannot bind to ZO proteins still formed TJ strands. ZO proteins were however necessary for cholesterol accumulation at the apical junctions through their effect on the junctional actomyosin cytoskeleton. We propose that ZO proteins not only function as scaffolds for claudins but also promote TJ formation of cholesterol-rich membrane domains at apical junctions.

    DOI: 10.1073/pnas.2217561120

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  • Tricellulin secures the epithelial barrier at tricellular junctions by interacting with actomyosin Reviewed International journal

    #Yuma Cho, #Daichi Haraguchi, Kenta Shigetomi, Kenji Matsuzawa, Seiichi Uchida, Junichi Ikenouchi

    The Journal of Cell Biology   221 ( 4 )   2022.1   ISSN:0021-9525 eISSN:1540-8140

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:Journal of Cell Biology  

    The epithelial cell sheet functions as a barrier to prevent invasion of pathogens. It is necessary to eliminate intercellular gaps not only at bicellular junctions, but also at tricellular contacts, where three cells meet, to maintain epithelial barrier function. To that end, tight junctions between adjacent cells must associate as closely as possible, particularly at tricellular contacts. Tricellulin is an integral component of tricellular tight junctions (tTJs), but the molecular mechanism of its contribution to the epithelial barrier function remains unclear. In this study, we revealed that tricellulin contributes to barrier formation by regulating actomyosin organization at tricellular junctions. Furthermore, we identified α-catenin, which is thought to function only at adherens junctions, as a novel binding partner of tricellulin. α-catenin bridges tricellulin attachment to the bicellular actin cables that are anchored end-on at tricellular junctions. Thus, tricellulin mobilizes actomyosin contractility to close the lateral gap between the TJ strands of the three proximate cells that converge on tricellular junctions.

    DOI: 10.1083/jcb.202009037

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  • mTORC2 suppresses cell death induced by hypo-osmotic stress by promoting sphingomyelin transport Reviewed International journal

    #Yumiko Ono, Kenji Matsuzawa, Junichi Ikenouchi

    The Journal of Cell Biology   221 ( 4 )   2022.1   ISSN:0021-9525 eISSN:1540-8140

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    Language:English   Publishing type:Research paper (scientific journal)   Publisher:Journal of Cell Biology  

    Epithelial cells are constantly exposed to osmotic stress. The influx of water molecules into the cell in a hypo-osmotic environment increases plasma membrane tension as it rapidly expands. Therefore, the plasma membrane must be supplied with membrane lipids since expansion beyond its elastic limit will cause the cell to rupture. However, the molecular mechanism to maintain a constant plasma membrane tension is not known. In this study, we found that the apical membrane selectively expands when epithelial cells are exposed to hypo-osmotic stress. This requires the activation of mTORC2, which enhances the transport of secretory vesicles containing sphingomyelin, the major lipid of the apical membrane. We further show that the mTORC2-Rab35 axis plays an essential role in the defense against hypotonic stress by promoting the degradation of the actin cortex through the up-regulation of PI(4,5)P2 metabolism, which facilitates the apical tethering of sphingomyelin-loaded vesicles to relieve plasma membrane tension.

    DOI: 10.1083/jcb.202106160

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  • STIM-Orai1 signaling regulates fluidity of cytoplasm during membrane blebbing. International journal

    Kana Aoki, Shota Harada, Keita Kawaji, Kenji Matsuzawa, Seiichi Uchida, Junichi Ikenouchi

    Nature communications   12 ( 1 )   480 - 480   2021.1

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    The cytoplasm in mammalian cells is considered homogeneous. In this study, we report that the cytoplasmic fluidity is regulated in the blebbing cells; the cytoplasm of rapidly expanding membrane blebs is more disordered than the cytoplasm of retracting blebs. The increase of cytoplasmic fluidity in the expanding bleb is caused by a sharp rise in the calcium concentration. The STIM-Orai1 pathway regulates this rapid and restricted increase of calcium in the expanding blebs. Conversely, activated ERM protein binds to Orai1 to inhibit the store-operated calcium entry in retracting blebs, which results in decreased in cytoplasmic calcium, rapid reassembly of the actin cortex.

    DOI: 10.1038/s41467-020-20826-5

  • PAR3-aPKC regulates Tiam1 by modulating suppressive internal interactions. Invited Reviewed International journal

    Kenji Matsuzawa, Hiroki Akita, Takashi Watanabe, Mai Kakeno, Toshinori Matsui, Shujie Wang, Kozo Kaibuchi

    Molecular biology of the cell   27 ( 9 )   1511 - 23   2016.5

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    Tiam1 is one of the most extensively analyzed activators of the small GTPase Rac. However, fundamental aspects of its regulation are poorly understood. Here we demonstrate that Tiam1 is functionally suppressed by internal interactions and that the PAR complex participates in its full activation. The N-terminal region of Tiam1 binds to the protein-binding and catalytic domains to inhibit its localization and activation. Atypical PKCs phosphorylate Tiam1 to relieve its intramolecular interactions, and the subsequent stabilization of its interaction with PAR3 allows it to exert localized activity. By analyzing Tiam1 regulation by PAR3-aPKC within the context of PDGF signaling, we also show that PAR3 directly binds PDGF receptor β. Thus we provide the first evidence for the negative regulation of Tiam1 by internal interactions, elucidate the nature of Tiam1 regulation by the PAR complex, and reveal a novel role for the PAR complex in PDGF signaling.

    DOI: 10.1091/mbc.E15-09-0670

  • TTBK2 with EB1/3 regulates microtubule dynamics in migrating cells through KIF2A phosphorylation. International journal

    Takashi Watanabe, Mai Kakeno, Toshinori Matsui, Ikuko Sugiyama, Nariko Arimura, Kenji Matsuzawa, Aya Shirahige, Fumiyoshi Ishidate, Tomoki Nishioka, Shinichiro Taya, Mikio Hoshino, Kozo Kaibuchi

    The Journal of cell biology   210 ( 5 )   737 - 51   2015.8

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    Microtubules (MTs) play critical roles in various cellular events, including cell migration. End-binding proteins (EBs) accumulate at the ends of growing MTs and regulate MT end dynamics by recruiting other plus end-tracking proteins (+TIPs). However, how EBs contribute to MT dynamics through +TIPs remains elusive. We focused on tau-tubulin kinase 2 (TTBK2) as an EB1/3-binding kinase and confirmed that TTBK2 acted as a +TIP. We identified MT-depolymerizing kinesin KIF2A as a novel substrate of TTBK2. TTBK2 phosphorylated KIF2A at S135 in intact cells in an EB1/3-dependent fashion and inactivated its MT-depolymerizing activity in vitro. TTBK2 depletion reduced MT lifetime (facilitated shrinkage and suppressed rescue) and impaired HeLa cell migration, and these phenotypes were partially restored by KIF2A co-depletion. Expression of nonphosphorylatable KIF2A, but not wild-type KIF2A, reduced MT lifetime and slowed down the cell migration. These findings indicate that TTBK2 with EB1/3 phosphorylates KIF2A and antagonizes KIF2A-induced depolymerization at MT plus ends for cell migration.

    DOI: 10.1083/jcb.201412075

  • PAR3 and aPKC regulate Golgi organization through CLASP2 phosphorylation to generate cell polarity. International journal

    Toshinori Matsui, Takashi Watanabe, Kenji Matsuzawa, Mai Kakeno, Nobumasa Okumura, Ikuko Sugiyama, Norimichi Itoh, Kozo Kaibuchi

    Molecular biology of the cell   26 ( 4 )   751 - 61   2015.2

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    The organization of the Golgi apparatus is essential for cell polarization and its maintenance. The polarity regulator PAR complex (PAR3, PAR6, and aPKC) plays critical roles in several processes of cell polarization. However, how the PAR complex participates in regulating the organization of the Golgi remains largely unknown. Here we demonstrate the functional cross-talk of the PAR complex with CLASP2, which is a microtubule plus-end-tracking protein and is involved in organizing the Golgi ribbon. CLASP2 directly interacted with PAR3 and was phosphorylated by aPKC. In epithelial cells, knockdown of either PAR3 or aPKC induced the aberrant accumulation of CLASP2 at the trans-Golgi network (TGN) concomitantly with disruption of the Golgi ribbon organization. The expression of a CLASP2 mutant that inhibited the PAR3-CLASP2 interaction disrupted the organization of the Golgi ribbon. CLASP2 is known to localize to the TGN through its interaction with the TGN protein GCC185. This interaction was inhibited by the aPKC-mediated phosphorylation of CLASP2. Furthermore, the nonphosphorylatable mutant enhanced the colocalization of CLASP2 with GCC185, thereby perturbing the Golgi organization. On the basis of these observations, we propose that PAR3 and aPKC control the organization of the Golgi through CLASP2 phosphorylation.

    DOI: 10.1091/mbc.E14-09-1382

  • Tiam1 interaction with the PAR complex promotes talin-mediated Rac1 activation during polarized cell migration. International journal

    Shujie Wang, Takashi Watanabe, Kenji Matsuzawa, Akira Katsumi, Mai Kakeno, Toshinori Matsui, Feng Ye, Kazuhide Sato, Kiyoko Murase, Ikuko Sugiyama, Kazushi Kimura, Akira Mizoguchi, Mark H Ginsberg, John G Collard, Kozo Kaibuchi

    The Journal of cell biology   199 ( 2 )   331 - 45   2012.10

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    Migrating cells acquire front-rear polarity with a leading edge and a trailing tail for directional movement. The Rac exchange factor Tiam1 participates in polarized cell migration with the PAR complex of PAR3, PAR6, and atypical protein kinase C. However, it remains largely unknown how Tiam1 is regulated and contributes to the establishment of polarity in migrating cells. We show here that Tiam1 interacts directly with talin, which binds and activates integrins to mediate their signaling. Tiam1 accumulated at adhesions in a manner dependent on talin and the PAR complex. The interactions of talin with Tiam1 and the PAR complex were required for adhesion-induced Rac1 activation, cell spreading, and migration toward integrin substrates. Furthermore, Tiam1 acted with talin to regulate adhesion turnover. Thus, we propose that Tiam1, with the PAR complex, binds to integrins through talin and, together with the PAR complex, thereby regulates Rac1 activity and adhesion turnover for polarized migration.

    DOI: 10.1083/jcb.201202041

  • Numb controls E-cadherin endocytosis through p120 catenin with aPKC. International journal

    Kazuhide Sato, Takashi Watanabe, Shujie Wang, Mai Kakeno, Kenji Matsuzawa, Toshinori Matsui, Keiko Yokoi, Kiyoko Murase, Ikuko Sugiyama, Masayuki Ozawa, Kozo Kaibuchi

    Molecular biology of the cell   22 ( 17 )   3103 - 19   2011.9

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    Cadherin trafficking controls tissue morphogenesis and cell polarity. The endocytic adaptor Numb participates in apicobasal polarity by acting on intercellular adhesions in epithelial cells. However, it remains largely unknown how Numb controls cadherin-based adhesion. Here, we found that Numb directly interacted with p120 catenin (p120), which is known to interact with E-cadherin and prevent its internalization. Numb accumulated at intercellular adhesion sites and the apical membrane in epithelial cells. Depletion of Numb impaired E-cadherin internalization, whereas depletion of p120 accelerated internalization. Expression of the Numb-binding fragment of p120 inhibited E-cadherin internalization in a dominant-negative fashion, indicating that Numb interacts with the E-cadherin/p120 complex and promotes E-cadherin endocytosis. Impairment of Numb induced mislocalization of E-cadherin from the lateral membrane to the apical membrane. Atypical protein kinase C (aPKC), a member of the PAR complex, phosphorylated Numb and inhibited its association with p120 and α-adaptin. Depletion or inhibition of aPKC accelerated E-cadherin internalization. Wild-type Numb restored E-cadherin internalization in the Numb-depleted cells, whereas a phosphomimetic mutant or a mutant with defective α-adaptin-binding ability did not restore the internalization. Thus, we propose that aPKC phosphorylates Numb to prevent its binding to p120 and α-adaptin, thereby attenuating E-cadherin endocytosis to maintain apicobasal polarity.

    DOI: 10.1091/mbc.E11-03-0274

  • Phosphorylation of CLASP2 by GSK-3beta regulates its interaction with IQGAP1, EB1 and microtubules. International journal

    Takashi Watanabe, Jun Noritake, Mai Kakeno, Toshinori Matsui, Takumi Harada, Shujie Wang, Norimichi Itoh, Kazuhide Sato, Kenji Matsuzawa, Akihiro Iwamatsu, Niels Galjart, Kozo Kaibuchi

    Journal of cell science   122 ( Pt 16 )   2969 - 79   2009.8

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    Polarised cell migration is required for various cell behaviours and functions. Actin and microtubules are coupled structurally and distributed asymmetrically along the front-rear axis of migrating cells. CLIP-associating proteins (CLASPs) accumulate near the ends of microtubules at the front of migrating cells to control microtubule dynamics and cytoskeletal coupling. Regional inhibition of GSK-3beta is responsible for this asymmetric distribution of CLASPs. However, it is not known how GSK-3beta regulates the activity of CLASPs for linkage between actin and microtubules. Here we identified IQGAP1, an actin-binding protein, as a novel CLASP-binding protein. GSK-3beta directly phosphorylates CLASP2 at Ser533 and Ser537 within the region responsible for the IQGAP1 binding. Phosphorylation of CLASP2 results in the dissociation of CLASP2 from IQGAP1, EB1 and microtubules. At the leading edges of migrating fibroblasts, CLASP2 near microtubule ends partially colocalises with IQGAP1. Expression of active GSK-3beta abrogates the distribution of CLASP2 on microtubules, but not that of a nonphosphorylatable CLASP2 mutant. The phosphorylated CLASP2 does not accumulate near the ends of microtubules at the leading edges. Thus, phosphorylation of CLASP2 by GSK-3beta appears to control the regional linkage of microtubules to actin filaments through IQGAP1 for cell migration.

    DOI: 10.1242/jcs.046649

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Presentations

  • Extracellular vesicles in epithelial cell homeostasis 上皮細胞シートの恒常性における細胞外小胞の役割

    松沢健司、池ノ内順一

    第75回日本細胞生物学会大会  2023.6 

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    Event date: 2023.6

    Language:Japanese   Presentation type:Symposium, workshop panel (public)  

    Venue:奈良県コンベンションセンター   Country:Japan  

  • Extracellular vesicles in epithelial cell homeostasis 上皮細胞シートの恒常性における細胞外小胞の役割

    松沢健司, 池ノ内順一

    第75回日本細胞生物学会大会  2023.6 

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    Event date: 2023.6

    Language:Japanese  

    Venue:奈良県コンベンションセンター   Country:Japan  

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  • Homer mobilizes calcium signaling to enable rapid restoration of epithelial cell sheet homeostasis

    Kenji Matsuzawa, #Ryoya Fujinaga, #Yuma Cho, Junichi Ikenouchi

    第74回日本細胞生物学会大会  2022.6 

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    Event date: 2022.6

    Language:Japanese   Presentation type:Symposium, workshop panel (public)  

    Venue:東京都   Country:Japan  

  • Homer mobilizes calcium signaling to enable rapid restoration of epithelial cell sheet homeostasis

    Kenji Matsuzawa, Ryoya Fujinaga, Yuma Cho, Junichi Ikenouchi

    第74回日本細胞生物学会大会  2022.6 

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    Language:Japanese  

    Venue:東京都   Country:Japan  

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  • Epithelial adhesions modulate apical domain contraction to drive cell shape change International conference

    Kenji Matsuzawa, Junichi Ikenouchi

    The 51st NIPS International Symposium "Frontiers in Epithelial Cell Biology"  2021.12 

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    Event date: 2021.12 - 2022.6

    Language:English   Presentation type:Symposium, workshop panel (public)  

    Venue:オンライン   Country:Japan  

  • Epithelial adhesions modulate apical domain contraction to drive cell shape change International conference

    Kenji Matsuzawa, Junichi Ikenouchi

    The 51st NIPS International Symposium "Frontiers in Epithelial Cell Biology"  2021.12 

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    Event date: 2021.12 - 2022.6

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    Venue:オンライン   Country:Japan  

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  • MAGI-ASPPを介した細胞の収縮力調節による上皮細胞シートの恒常性維持機構

    松沢健司、池ノ内順一

    日本細胞生物学会  2021.7 

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    Event date: 2021.6 - 2021.7

    Language:Japanese   Presentation type:Oral presentation (general)  

    Venue:オンライン   Country:Japan  

    Multicellular tissues are covered by a continuous sheet of epithelial cells. The epithelial cells adhere to each other through cell adhesion structures, the apical junctional complexes (AJC), that are reinforced by a network of actomyosin filaments. Contractility of the actomyosin network drives the constriction of the apical plasma membrane, a hallmark of epithelial cells that underlies cell shape changes during developmental morphogenesis and maintenance of tissue integrity in homeostasis. However, it is unclear how the core components of the AJC modulate apical contractility in the broader context of the epithelial cell sheet.
    In this study, we present evidence that the membrane-associated guanylate kinases (MAGUK) family proteins MAGI-1 and MAGI-3 are key negative regulators of apical membrane contractility. We find that MAGI knockout in a model epithelial cell line enriches non-muscle myosin IIB (NMIIB) as well as the myosin activator Rho-associated protein kinase 1 (ROCK1) at AJC. As a result of the heightened cellular contractility, the MAGI knockout cell sheet is populated by cells having irregularly sized apical domains. Members of MAGI proteins are differentially recruited to the AJC by the scaffolding proteins afadin and the zonula occludens (ZO) family proteins. MAGI then recruit ankyrin-repeat-, SH3-domain- and proline-rich-region-containing protein 2 (ASPP2), which in turn controls the localizations of the polarity proteins Partitioning defective-3 (Par-3) and atypical protein kinase C (aPKC) at AJC. We further clarify the functional interaction between ASPP2 and Par-3 by elucidating the requirement for ASPP2 recruitment of protein phosphatase 1 (PP1) to retain aPKC at AJC, which is necessary to antagonize ROCK. These results taken together indicate that homeostasis of the epithelial sheet morphology requires conformity of two factors within a certain range by the constituent cells: junctional ROCK activity and NMIIB recruitment. Finally, signaling from AJC to Par-3-aPKC through MAGI is a crucial means of normalizing this activity level, owing to MAGIs’ role in regulating local phosphorylation dynamics through ASPP2-PP1.

  • 上皮細胞極性における接着タンパク質ZOとafadinの相乗的作用の解析

    松沢健司、#大賀隼人、池ノ内順一

    第42回日本分子生物学会年会  2019.12 

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    Event date: 2019.12

    Language:Japanese  

    Venue:福岡市   Country:Japan  

  • Alpha-catenin controls the anisotropy of force distribution at cell-cell junctions during collective cell migration

    Kenji Matsuzawa, #Takuya Himoto, #Yuki Mochizuki, Junichi Ikenouchi

    第70回日本細胞生物学会・第51回日本発生生物学会合同大会  2018.6 

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    Event date: 2019.6

    Language:English  

    Venue:東京   Country:Japan  

  • アルファカテニンによる集団細胞運動の制御機構

    松沢健司

    新学術領域「数理シグナル」第2回若手ワークショップ  2018.9 

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    Event date: 2019.6

    Language:Japanese   Presentation type:Symposium, workshop panel (public)  

    Country:Japan  

  • タイトジャンクション形成においてコレステロールの集積が果たす役割の解明

    重富 健太, 小野 由美子, 松沢 健司, 池ノ内 順一

    日本生化学会大会プログラム・講演要旨集  2023.10  (公社)日本生化学会

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    Language:Japanese  

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Professional Memberships

  • Japan Society for Cell Biology

  • The Molecular Biology Society of Japan

  • Japan Society for Cell Biology

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  • The Molecular Biology Society of Japan

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Academic Activities

  • Screening of academic papers

    Role(s): Peer review

    2023

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    Type:Peer review 

    Number of peer-reviewed articles in foreign language journals:3

  • Screening of academic papers

    Role(s): Peer review

    2022

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    Type:Peer review 

    Number of peer-reviewed articles in foreign language journals:3

  • 座長

    第73回日本細胞生物学会大会  ( Japan ) 2021.6 - 2021.7

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    Type:Competition, symposium, etc. 

  • Screening of academic papers

    Role(s): Peer review

    2021

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    Type:Peer review 

    Number of peer-reviewed articles in foreign language journals:1

  • Screening of academic papers

    Role(s): Peer review

    2020

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    Type:Peer review 

    Number of peer-reviewed articles in foreign language journals:1

Research Projects

  • 運動性の細胞集団が秩序を獲得するまでの分子メカニズムの解明

    Grant number:22K06225  2022 - 2024

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (C)

    松沢 健司

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    Authorship:Principal investigator  Grant type:Scientific research funding

    上皮組織の恒常性は、様々な生命現象が協調的に進行することにより支えられている。上皮細胞シートや血管内皮細胞など細胞が互いに接着して細胞集団を形成する組織では、細胞間で絶えず張力が発揮されており、組織内の個々の細胞には組織全体にかかる力に適切に応答する能力が求められる。申請者はこれまでに、集団細胞運動や上皮細胞シートの恒常性などの協調的な応答を必要とする細胞集団の振る舞いについて、細胞間張力の制御という視点から研究を進めてきた。本研究提案では、細胞間に働く力がもたらす細胞接着の可塑的変化を基軸に、「集団を構成する細胞がどのような分子機構で協調性を獲得しているか」、という問題の解明を目指す。

    CiNii Research

  • 集団細胞運動における細胞接着の可塑性の制御と役割

    Grant number:19K06640  2019 - 2021

    Japan Society for the Promotion of Science  Grants-in-Aid for Scientific Research  Grant-in-Aid for Scientific Research (C)

    松沢 健司

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    Authorship:Principal investigator  Grant type:Scientific research funding

    上皮細胞が接着を維持しながら運動する様式を集団細胞運動と呼ぶ。集団細胞運動は、正常発生過程のみならず、がん細胞の浸潤・転移の過程でも観察され。個々の細胞が自由に運動する場合と異なり、細胞集団が効率良く運動するためには、集団を形成する細胞が運動の方向性やスピードを協調させる必要がある。本研究提案では、張力依存的に起こるAJの構成要素のリモデリングと細胞内生化学的シグナ ル(RhoAやERKの活性および細胞内Caイオンの変化)の間に存在するブラックボックスについて、最新の近位プロテオミクス技術およびイメージング技術を駆使し、集団細胞運動の全容解明を目指す。

    CiNii Research

  • 張力シグナルと生化学シグナルの相互制御による集団細胞運動の協調性確立メカニズム

    Grant number:18K14700  2018 - 2019

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

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    Authorship:Principal investigator  Grant type:Scientific research funding

Educational Activities

  • 基幹教育、理学部生物学科、大学院システム生命科学府の講義を受け持っている。
    また、学部生の卒業研究並びに大学院生の研究についても日常的に指導している。

Class subject

  • 分子細胞生物学

    2023.10 - 2024.3   Second semester

  • 分子生物学

    2023.4 - 2023.9   First semester

  • 生物科学I

    2023.4 - 2023.9   First semester

  • 自然科学総合実験

    2023.4 - 2023.6   Spring quarter

  • 分子細胞生物学

    2022.10 - 2023.3   Second semester

  • 生物科学特論Ⅱ

    2022.6 - 2022.8   Summer quarter

  • Biology, Advanced CouresⅡ

    2022.6 - 2022.8   Summer quarter

  • 分子生物学

    2022.4 - 2022.9   First semester

  • Basic BiologyⅠ

    2022.4 - 2022.6   Spring quarter

  • 生物科学Ⅰ

    2022.4 - 2022.6   Spring quarter

  • 分子細胞生物学

    2021.10 - 2022.3   Second semester

  • 分子生物学

    2021.4 - 2021.9   First semester

  • Basic BiologyⅠ

    2021.4 - 2021.6   Spring quarter

  • 生物科学Ⅰ

    2021.4 - 2021.6   Spring quarter

  • 分子細胞生物学

    2020.10 - 2021.3   Second semester

  • 応用生物化学実験

    2020.10 - 2021.3   Second semester

  • 分子生物学

    2020.4 - 2020.9   First semester

  • 分子生命科学I

    2020.4 - 2020.6   Spring quarter

  • 応用生物化学実験

    2019.4 - 2019.9   First semester

  • 自然科学総合実験

    2019.4 - 2019.9   First semester

  • 応用生物化学実験

    2019.4 - 2019.9   First semester

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FD Participation

  • 2023.3   Role:Participation   Title:【生物学科】大学発明の出願・権利化に関するFD

    Organizer:Undergraduate school department

  • 2022.3   Role:Participation   Title:【生物学科】入学者選抜試験に関するFD

    Organizer:Undergraduate school department

  • 2016.8   Role:Participation   Title:障害者支援に関する教職員FD

    Organizer:[Undergraduate school/graduate school/graduate faculty]

Outline of Social Contribution and International Cooperation activities

  • オープンキャンパスでは高校生及び保護者を対象に研究室を公開している。