Matsuda, Keiko

写真a

Affiliation

School of Medicine, Department of Physiology (Shinanomachi)

Position

Assistant Professor/Senior Assistant Professor

Career 【 Display / hide

  • 2004.04
    -
    2008

    Keio University, School of Medicine,, Dept. of Physiology 1, 助手

  • 2008
    -
    2015.09

    Keio University, School of Medicine,, Dept. of Physiology 1, 助教

  • 2015.09
    -
    2016.09

    Keio University, School of Medicine,, Dept. of Physiology 1, 講師(学部内)

  • 2016.10
    -
    Present

    School of Medicine, 生理学, 専任講師

Academic Background 【 Display / hide

  •  

    Osaka University, 医学部

Academic Degrees 【 Display / hide

  • 医学博士, 大阪大学医学部, Dissertation, 2001.06

 

Research Areas 【 Display / hide

  • General physiology

Research Keywords 【 Display / hide

  • Neuroscience

 

Papers 【 Display / hide

  • A synthetic synaptic organizer protein restores glutamatergic neuronal circuits

    Suzuki K., Elegheert J., Song I., Sasakura H., Senkov O., Matsuda K., Kakegawa W., Clayton A.J., Chang V.T., Ferrer-Ferrer M., Miura E., Kaushik R., Ikeno M., Morioka Y., Takeuchi Y., Shimada T., Otsuka S., Stoyanov S., Watanabe M., Takeuchi K., Dityatev A., Radu Aricescu A., Yuzaki M.

    Science (Science)  369 ( 6507 )  2020.08

    ISSN  00368075

     View Summary

    Copyright © 2020 The Authors, Neuronal synapses undergo structural and functional changes throughout life, which are essential for nervous system physiology. However, these changes may also perturb the excitatory–inhibitory neurotransmission balance and trigger neuropsychiatric and neurological disorders. Molecular tools to restore this balance are highly desirable. Here, we designed and characterized CPTX, a synthetic synaptic organizer combining structural elements from cerebellin-1 and neuronal pentraxin-1. CPTX can interact with presynaptic neurexins and postsynaptic AMPA-type ionotropic glutamate receptors and induced the formation of excitatory synapses both in vitro and in vivo. CPTX restored synaptic functions, motor coordination, spatial and contextual memories, and locomotion in mouse models for cerebellar ataxia, Alzheimer’s disease, and spinal cord injury, respectively. Thus, CPTX represents a prototype for structure-guided biologics that can efficiently repair or remodel neuronal circuits.

  • Calsyntenin-3 interacts with both α- and β-neurexins in the regulation of excitatory synaptic innervation in specific Schaffer collateral pathways

    Kim H., Kim D., Kim J., Lee H.Y., Park D., Kang H., Matsuda K., Sterky F.H., Yuzaki M., Kim J.Y., Choi S.Y., Ko J., Um J.W.

    The Journal of biological chemistry (The Journal of biological chemistry)  295 ( 27 ) 9244 - 9262 2020.07

     View Summary

    © 2020 Kim et al. Calsyntenin-3 (Clstn3) is a postsynaptic adhesion molecule that induces presynaptic differentiation via presynaptic neurexins (Nrxns), but whether Nrxns directly bind to Clstn3 has been a matter of debate. Here, using LC-MS/MS-based protein analysis, confocal microscopy, RNAscope assays, and electrophysiological recordings, we show that β-Nrxns directly interact via their LNS domain with Clstn3 and Clstn3 cadherin domains. Expression of splice site 4 (SS4) insert-positive β-Nrxn variants, but not insert-negative variants, reversed the impaired Clstn3 synaptogenic activity observed in Nrxn-deficient neurons. Consistently, Clstn3 selectively formed complexes with SS4-positive Nrxns in vivo Neuron-specific Clstn3 deletion caused significant reductions in number of excitatory synaptic inputs. Moreover, expression of Clstn3 cadherin domains in CA1 neurons of Clstn3 conditional knockout mice rescued structural deficits in excitatory synapses, especially within the stratum radiatum layer. Collectively, our results suggest that Clstn3 links to SS4-positive Nrxns to induce presynaptic differentiation and orchestrate excitatory synapse development in specific hippocampal neural circuits, including Schaffer collateral afferents.

  • Cellular and Subcellular Localization of Endogenous Neuroligin-1 in the Cerebellum

    Nozawa K., Hayashi A., Motohashi J., Takeo Y., Matsuda K., Yuzaki M.

    Cerebellum (Cerebellum)  17 ( 6 ) 709 - 721 2018.12

    ISSN  14734222

     View Summary

    © 2018, Springer Science+Business Media, LLC, part of Springer Nature. Synapses are precisely established, maintained, and modified throughout life by molecules called synaptic organizers, which include neurexins and neuroligins (Nlgn). Despite the importance of synaptic organizers in defining functions of neuronal circuits, the cellular and subcellular localization of many synaptic organizers has remained largely elusive because of the paucity of specific antibodies for immunohistochemical studies. In the present study, rather than raising specific antibodies, we generated knock-in mice in which a hemagglutinin (HA) epitope was inserted in the Nlgn1 gene. We have achieved high-throughput and precise gene editing by delivering the CRISPR/Cas9 system into zygotes. Using HA-Nlgn1 mice, we found that HA-Nlgn1 was enriched at synapses between parallel fibers and molecular layer interneurons (MLIs) and the glomeruli, in which mossy fiber terminals synapse onto granule cell dendrites. HA immunoreactivity was colocalized with postsynaptic density 95 at these synapses, indicating that endogenous Nlgn1 is localized at excitatory postsynaptic sites. In contrast, HA-Nlgn1 signals were very weak in dendrites and somata of Purkinje cells. Interestingly, HA-immunoreactivities were also observed in the pinceau, a specialized structure formed by MLI axons and astrocytes. HA-immunoreactivities in the pinceau were significantly reduced by knockdown of Nlgn1 in MLIs, indicating that in addition to postsynaptic sites, Nlgn1 is also localized at MLI axons. Our results indicate that epitope-tagging by electroporation-based gene editing with CRISPR/Cas9 is a viable and powerful method for mapping endogenous synaptic organizers with subcellular resolution, without the need for specific antibodies for each protein.

  • Synapse organization and modulation via C1 q family proteins and their receptors in the central nervous system

    Matsuda, Keiko

    NEUROSCIENCE RESEARCH 116   46 - 53 2017.03

    Research paper (scientific journal),  ISSN  0168-0102

  • Structural basis for integration of GluD receptors within synaptic organizer complexes

    Elegheert, Jonathan, Kakegawa, Wataru, Clay, Jordan E., Shanks, Natalie F., Behiels, Ester, Matsuda, Keiko, Kohda, Kazuhisa, Miura, Eriko, Rossmann, Maxim, Mitakidis, Nikolaos, Motohashi, Junko, Chang, Veronica T., Siebold, Christian, Greger, Ingo H., Nakagawa, Terunaga, Yuzaki, Michisuke, Aricescu, A. Radu

    SCIENCE 353 ( 6296 ) 295 - 299 2016.07

    Research paper (scientific journal),  ISSN  0036-8075

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Papers, etc., Registered in KOARA 【 Display / hide

Presentations 【 Display / hide

  • Synapse organization and modulation via C1q family proteins and their receptors

    MATSUDA KEIKO

    第94回日本生理学会大会, 2017.03, Symposium, Workshop, Panelist (nomination)

  • Synaptic organization at CA3-mossy fiber synapse through novel C1q related molecules

    MATSUDA KEIKO

    第39回 日本神経科学大会, 2016.07, Oral Presentation(general)

  • Synapse organization and regulation through novel type of complement C1q family

    MATSUDA KEIKO

    第38回 日本神経科学大会, 2015.07, Symposium, Workshop, Panelist (public offering)

  • Cross talk between C1q family molecules and glutamate receptors in synapse formation

    MATSUDA KEIKO

    第36回日本神経科学会大会, 2013.06, Symposium, Workshop, Panelist (nomination)

  • Cbln1とその関連分子群によるシナプス形成

    MATSUDA KEIKO

    第34回日本神経科学会大会, 2011.09, Symposium, Workshop, Panelist (public offering)

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Research Projects of Competitive Funds, etc. 【 Display / hide

  • 補体様分泌因子とグルタミン酸受容体クロストークによるシナプス成熟の分子機構解明

    2017.04
    -
    2021.03

    MEXT,JSPS, Grant-in-Aid for Scientific Research, 松田 恵子, Grant-in-Aid for Scientific Research (B), Principal Investigator

  • The molecular mechanism of synapse organization and modulation via C1q family proteins

    2014.04
    -
    2017.03

    MEXT,JSPS, Grant-in-Aid for Scientific Research, 松田 恵子, Grant-in-Aid for Scientific Research (C), Principal Investigator

     View Summary

    Kainate-type ionotropic glutamate receptors (KARs) are highly expressed at synapses between mossy fibers (MFs) and CA3 pyramidal neurons in the hippocampus and important modulators of neural circuit activities. Although diverse KAR roles depend on their subcellular localization, how they are targeted to specific sites is currently unknown. We have demonstarated that the C1q-like proteins C1ql2 and C1ql3, produced by MFs, interact with the amino-terminal domains of postsynaptic GluK2 and GluK4 KAR subunits to determine location and function of KARs. In C1ql2/3-double null mice, CA3 synaptic responses lost the slow, KAR-mediated, components. Furthermore, despite induction of MF sprouting in a temporal lobe epilepsy model, KARs were not recruited to postsynaptic sites in C1ql2/3-double null mice, leading to reduced recurrent circuit activities. C1q-family proteins, broadly expressed, are likely to modulate KAR function throughout the brain.

 

Courses Taught 【 Display / hide

  • PHYSIOLOGY 1

    2021

  • PHYSIOLOGY 1

    2020

  • PHYSIOLOGY 1

    2019

Courses Previously Taught 【 Display / hide

  • 生理学Ⅰ

    Keio University, 2017, Full academic year, Major subject, Laboratory work/practical work/exercise

  • 生理学Ⅰ

    Keio University, 2017, Spring Semester, Major subject, Lecture

  • 生理学実習

    Keio University, 2015

  • 味覚 嗅覚

    Keio University, 2015

  • 聴覚

    Keio University, 2015

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Memberships in Academic Societies 【 Display / hide

  • Japan Neuroscience Society

     
  • Physiological Society of Japan

     
  • Society for Neuroscience